Abstract
Once a pathogen has penetrated the body there are two possible sites where replication can occur and where host defenses can mount a counterattack, namely, in intracellular or extracellular compartments. It is the job of B cells and the humoral arm of the immune system to manage the battle against extracellular stages of infection, to minimize the spread of infection, to antibody-label extracellular organisms and inactivate or target them for destruction, and to provide mechanisms of specific capture of antigen for presentation and support of T-cell responses—thereby providing a critical link between the humoral and cell-mediated arms of the immune system. The production of large amounts of clonotypic antibodies, or immunoglobulins (Ig), that both form membrane surface receptors and are secreted from B cells, is the cornerstone of the humoral response. The immunoglobulins are thus noted for their ability both to function as surface receptors on cells and to act as critical soluble mediators of adaptive immunity in blood and lymph.
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References
Greenberg, A. S., Steiner, L., Kasahara, M., and Flajnik, M. F. 1993. Isolation of a shark immunoglobulin light chain cDNA clone encoding a protein resembling mammalian kappa light chains: Implications for the evolution of light chains. Proc. Natl. Acad. Sci. USA 90:10603–10607.
Chen, J., and Alt, F. W. 1993. Gene rearrangement and B-cell development. Curr. Opin. Immunol. 5:194–200.
Maki, R., Roeder, W., Traunecker, A., Sidman, C., Wabl, M., Raschke, W., and Tonegawa, S. 1981. The role of DNA rearrangement and alternative RNA processing in the expression of immunoglobulin delta genes. Cell 24:353–365.
Haas, I. G., and Wabl, M. 1983. Immunoglobulin heavy chain binding protein. Nature 306:387–389.
Sitia, R., Neuberger, M. S., and Milstein, C. 1987. Regulation of membrane IgM expression in secretory B cells: Translational and post-translational events. EMBO J. 6:3969–3977.
Laussoued, K., Illges, H., Benlagha, K., and Cooper, M. D. 1996. Fate of surrogate light-chains in B-lineage cells. J. Exp. Med. 183:421–429.
Shirasawa, T., Ohnishi, K., Hagiwara, S., Shigemoto, K., Takebe, Y., Rajewsky, K., and Takemori, T. 1993. A novel gene product associated with mu chains in immature B cells. EMBO J. 12:1827–1834.
Grupp, S. A., Mitchell, R. N., Schreiber, K. L, McKean, D. J., and Abbas, A. K. 1995. Molecular mechanisms that control expression of the B lymphocyte antigen receptor complex. J. Exp. Med. 181:161–168.
Melnick, J., Aviel, S., and Argon, Y. 1992. The endoplasmic reticulum stress protein GRP94. in addition to BiP. associates with unassembled immunoglobulin chains. J. Biol. Chem. 267:21303–21306.
Melnick, J., Dul, J. L., and Argon, Y. 1994. Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum. Nature 370:373–375.
Brouns, G. S., de Vries, E., and Borst J. 1995. Assembly and intracellular transport of the human B cell antigen receptor complex. Int. Immunol. 7:359–368.
Melnick, J., and Argon, Y. 1995. Molecular chaperones and the biosynthesis of antigen receptors. Immunol. Today 16:243–250.
von Schwedler, U., Jaeck, H. M., and Wabl, M. 1990, Circular DNA is a product of the immunoglobulin class switch rearrangement. Nature 345:452–456.
Snapper, C. M., and Mond, J. J. 1993. Towards a comprehensive view of immunoglobulin class switching. Immunol. Today 14:15–17.
Harriman, W., Volk, H., Defranoux, N., and Wabl, M. 1993. Immunoglobulin class switch recombination. Annu. Rev. Immunol. 11:361–384.
Stavnezer, J., Abbott, J., and Sirlin, S. 1984. Immunoglobulin heavy chain switching in cultured 1.29 murine B lymphoma cells: Commitment to an IgA or IgE switch. Curr. Top. Microbiol. Immunol. 113:109–116.
Yancopoulos, G. D., DePinho, R. A., Zimmerman, K. A., Lutzker, S. G., Rosenberg, N., and Alt, F. W. 1986. Secondary genornic rearrangement events in pre-B cells: VHDJH replacement by a LINE-1 sequence and directed class switching. EMBO J. 5:3259–3266.
Stavnezer, J., Radcliffe, G., Lin, Y. C, Nietupski, J., Berggren, L., Sitia, R., and Severinson, E. 1988. Immunoglobulin heavy-chain switching may be directed by prior induction of transcripts from constant-region genes. Proc. Natl. Acad. Sci. USA 85:7704–7708.
Malisan, F., Briere, F., Bridon, J. M., Harindranath, N., Mills, F. C, Max, E. E., Banchereau, J., and Martinezvaldez, H. 1996. Interleukin-10 induces immunoglobulin-G isotype switch recombination in human CD40-activated naive B-lymphocytes. J. Exp. Med. 183:937–947.
Daniels, G. A., and Lieber, M. R. 1995. Strand specificity in the transcriptional targeting of recombination at immunoglobulin switch sequences. Proc. Natl. Acad. Sci. USA 92:5625–5629.
Michaelson, J. S., Singh, M., Snapper, C. M., Sha, W. C, Baltimore, D., and Birshtein, B. K. 1996. Regulation of 3’-lgH enhancers by a common set of factors, including kappa-B-binding proteins. J. Immunol. 156:2828–2839.
Yancopoulos, G. D., and Alt, F. W. 1986. Regulation of the assembly and expression of variable-region genes. Annu. Rev. Immunol. 4:339–368.
Cook, G. P., Tomlinson, I. M., Walter, G., Riethman, H., Carter, N. P., Buluwela, L., Winter, G., and Rabbitts, T. H. 1994. A map of the human immunoglobulin VH locus completed by analysis of the telomeric region of chromosome 14q. Nat. Genet. 7:162–168.
Tomlinson, I. M., Cook, G. P., Carter, N. P., Elaswarapu, R., Smith, S., Walter, G., Buluwela, L., Rabbins, T. H., and Winter, G. 1994. Human immunoglobulin VH and D segments on chromosomes 15qll.2 and 16pll.2. Hum. Mol. Genet. 3:853–860.
van Dijk, K. W., Mortari, F., Kirkham, P. M., Schroeder, H. W., Jr., and Milner, E. C. 1993. The human immunoglobulin VH7 gene family consists of a small, polymorphic group of six to eight gene segments dispersed throughout the VH locus. Eur. J. Immunol 23:832–839.
Kodaira, M., Kinashi, T., Umemura, I., Matsuda, F., Noma, T., Ono, Y., and Honjo, T. 1986. Organization and evolution of variable region genes of the human immunoglobulin heavy chain. J. Mol. Biol. 190:529–541.
Berman, J. E., Mellis, S. J., Pollock, R., Smith, C. L., Suh, H., Heinke, B., Kowal, C, Surti, U., Chess, L., Cantor, C. R., and Alt, F. 1988. Content and organization of the human Ig VH locus: Definition of three new VH families and linkage to the Ig CH locus. EMBO J. 7:727–738.
Matsuda, F., Shin, E. K., Nagaoka, H., Matsumura, R., Haino, M., Fukita, Y., Takaishi, S., Imai, T., Riley, J. H., Anand, R., Soeda, E., and Honjo, T. 1993. Structure and physical map of 64 variable segments in the 3’ 0.8-megabase region of the human immunoglobulin heavy-chain locus. Nat. Genet. 3:88–94.
Kofler, R., Geley, S., Kofler, H., and Helmberg, A. 1992. Mouse variable-region gene families: Complexity, polymorphism and use in non-autoimmune responses. Immunol. Rev. 128:5–21.
Rathbun, G. A., Capra, J. D., and Tucker, P. W. 1987. Organization of the murine immunoglobulin VH complex in the inbred strains. EMBO J. 6:2931–2937.
Blankcnstein, T., and Krawinkel, U. 1987. Immunoglobulin VH region genes of the mouse are organized in overlapping clusters. Eur. J. Immunol. 17:1351–1357.
Haino, M., Hayashida, H., Miyata, T., Shin, E. K., Matsuda, F., Nagaoka, H., Matsumura, R., Takaishi, S., Fukita, Y., Fujikura, J., and Honjo, T. 1994. Comparison and evolution of human immunoglobulin VH segments located in the 3’ 0.8-megabase region. Evidence for unidirectional transfer of segmental gene sequences. J. Biol. Chem. 269:2619–2626.
Nagaoka, H., Ozawa, K., Matsuda, F., Hayashida, H., Malsumura, R., Haino, M., Shin, E. K., Fukita, Y., Imai, T., Anand, R., Yokoyama, K., Eki, T., Soeda, E., and Honjo, T. 1994. Recent translocation of variable and diversity segments of the human immunoglobulin heavy chain from chromosome 14 to chromosomes 15 and 16. Genomics 22:189–197.
Kocher, H. P., Bijlenga, R. K., and Jaton, J. C. 1982. Biosynthesis and structure of membrane and secretory immunoglobulins. Mol. Cell Biochem. 47:11–22.
Rogers, J., Choi, E., Souza, L., Carter, C, Word, C, Kuehl, M., Eisenberg, D., and Wall, R. 1981. Gene segments encoding transmembrane carboxyl termini of immunoglobulin gamma chains. Cell 26:19–27.
Tsurushita, N., and Korn, L. J. 1987. Effects of intron length on differential processing of mouse mu heavychain mRNA. Mol. Cell. Biol. 7:2602–2605.
Watakabe, A., Tanaka, K., and Shimura, Y. 1993. The role of exon sequences in splice site selection. Genes Dev. 7:407–418.
Tanaka, K., Watakabe, A., and Shimura, Y. 1994. Polypurine sequences within a downstream exon function as a splicing enhancer. Mol. Cell. Biol 14:1347–1354.
Tsurushita, N., Avdalovic, N. M., and Korn, L. J. 1987. Regulation of differential processing of mouse immunoglobulin mu heavy-chain mRNA. Nucleic Acids Res. 15:4603–4615.
Zachau, H. G. 1993. The immunoglobulin kappa locus—or—what has been learned from looking closely at one-tenth of a percent of the human genome. Gene 135:167–173.
Malcolm, S., Barton, P., Murphy, C, Ferguson-Smith, M. A., Bentley, D. L., and Rabbitts, T. H. 1982. Localization of human immunoglobulin kappa light chain variable region genes to the short arm of chromosome 2 by in situ hybridization. Proc. Natl. Acad. Sci. USA 79:4957–4961.
McBride, O. W., Hieter, P. A., Hollis, G. F., Swan, D., Otey, M. C, and Leder, P. 1982. Chromosomal location of human kappa and lambda immunoglobulin light chain constant region genes. J. Exp. Med. 155:1480–1490.
Demaison, C, David, D., and Theze, J. 1995. Analysis of the human vh gene repertoire expressed by peripheral CD19(+) B-cells reveals a strong bias usage in normal and pathological situations. FASEB J. 9:PA1032.
Arnold, N., Wienberg, J., Ermert, K., and Zachau, H. G. 1995. Comparative mapping of DNA probes derived from the V-K immunoglobulin gene regions on human and great ape chromosomes by fluorescence in-situ hybridization. Genomics 26:147–150.
Zocher, I., Roschenthaler, F., Kirschbaum, T., Schable, K. F., Horlein, R., Fleischmann, B., Kofler, R., Geley, S., Hameister, H., and Zachau, H. G. 1995. Clustered and interspersed gene families in the mouse immunoglobulin-chi locus. Eur. J. Immunol. 25:3326–3331.
Chen, J., Trounstine, M., Kurahara, C, Young, F., Kuo, C. C, Xu, Y., Loring, J. F., Alt, F. W., and Huszar, D. 1993. B cell development in mice that lack one or both immunoglobulin kappa light chain genes. EMBO J. 12:821–830.
Zou, Y. R., Takeda, S., and Rajewsky, K. 1993. Gene targeting in the Ig kappa locus: Efficient generation of lambda chain-expressing B cells, independent of gene rearrangements in Ig kappa. EMBO J. 12:811–820.
Vasicek, T. J., and Leder, P. 1990. Structure and expression of the human immunoglobulin lambda genes. J. Exp. Med. 172:609–620.
Ramsden, D. A., and Wu, G. E. 1991. Mouse kappa light-chain recombination signal sequences mediate recombination more frequently than do those of lambda light chain. Proc. Natl. Acad. Sci. USA 88:10721–10725.
Conn, M., and Langman, R. E. 1990. The protection: The unit of humoral immunity selected by evolution. Immunol. Rev. 115:11–147.
Sanchez, P., Drapier, A. M., Cohen Tannoudji, M, Colucci, E., Babinet, C, and Cazenave, P. A 1994. Compartmentalization of lambda subtype expression in the B cell repertoire of mice with a disrupted or normal C kappa gene segment. Int. Immunol. 6:711–719.
Takeda, S., Zou, Y. R., Bluethmann, H., Kitamura, D., Muller, U., and Rajewsky, K. 1993. Deletion of the immunoglobulin kappa chain intron enhancer abolishes kappa chain gene rearrangement in cis but not lambda chain gene rearrangement in trans. EMBO J. 12:2329–2336.
Giachino, C., Padovan, E., and Lanzavecchia, A. 1995. Kappa(+)lambda(+) dual receptor B-cells are present in the human peripheral repertoire. J. Exp. Med. 181:1245–1250.
Victor, K. D., and Capra, J. D. 1994. An apparently common mechanism of generating antibody diversity-Length variation of the VL-JL junction. Mol. Immunol. 31:39–46.
Gilfillan, S., Bachmann, M., Trembleau, S., Adorini, L., Kalinke, U., Zinkernagel, R., Benoist, C. and Mathis, D. 1995. Efficient immune responses in mice lacking N-region diversity. Eur. J. Immunol. 25:3115–3122.
Kwan, S. P., Max, E. E., Seidman, J. G., Leder, P., and Scharff, M. D. 1981. Two kappa immunoglobulin genes are expressed in the myeloma S107. Cell 26:57–66.
Ritchie, K. A., Brinster, R. L., and Storb, U. 1984. Allelic exclusion and control of endogenous immunoglobulin gene rearrangement in kappa transgenic mice. Nature 312:517–520.
Storb, U. 1987. Transgenic mice with immunoglobulin genes. Annu. Rev. Immunol. 5:151–174.
Gay, D., Saunders, T., Camper, S., and Weigert, M. 1993. Receptor editing: An approach by auloreaclive B cells to escape tolerance. J. Exp. Med. 177:1009–1020.
Tiegs, S. L., Russell, D. M., and Nemazee, D. 1993. Receptor editing in self-reactive bone marrow B cells. J. Exp. Med. 177:1009–1020.
Prak, E. L., and Weigert, M. 1995. Light chain replacement: A new model for antibody gene rearrangement. J. Exp. Med. 182:541–548.
Prak, E. L., Trounstine, M., Huszar, D., and Weigert, M. 1994. Light chain editing in kappa-deficient animals: A potential mechanism of B cell tolerance. J. Exp. Med. 180:1805–1815.
Ferradini, L., Gu, H., Desmet, A., Rajewsky, K., Reynaud, C. A., and Weill, J. C. 1996. Rearrangement-enhancing element upstream of the mouse immunoglobulin-kappa chain J-cluster. Science 271:1416–1420.
Chuchana, P., Blancher, A., Brockly, F., Alexandre, D., Lefranc, G., and LeFranc, M. P. 1990. Definition of the human immunoglobulin variable lambda (IGLV) gene subgroups. Eur. J. Immunol. 20:1317–1325.
Williams, S. C, and Winter, G. 1993. Cloning and sequencing of human immunoglobulin V lambda gene segments. Eur. J. Immunol. 23:1456–1461.
Stiernholm, N. B., Kuzniar, B., and Berinstein, N. L. 1994. Identification of a new human V lambda gene family V lambda X. J. Immunol. 152:4969–4975.
Frippiat, J. P., Williams, S. C, Tomlinson, I. M., Cook, G. P., Cherif, D., Lepaslier, D., Collins, J. E., Dunham, I., Winter, G., and LeFranc, M. P. 1995. Organization of the human-immunoglobulin lambda-light-chain locus on chromosome 22q11.2. Hum. Mol. Genet. 4:983–991.
Lai, E., Wilson, R. K., and Hood, L. E. 1989. Physical maps of the mouse and human immunoglobulin-like loci. Adv. Immunol. 46:1–59.
Combriato, G., and Klobeck, H. G. 1991. V lambda and J lambda-C lambda gene segments of the human immunoglobulin lambda light chain locus are separated by 14 kb and rearrange by a deletion mechanism. Eur. J. Immunol. 21:1513–1522.
Asenbauer, H., and Klobeck, H. G. 1996. Tissue-specific deoxyribonuclease 1-hypersensitive sites in the vicinity of the immunoglobulin c-lambda cluster of man. Eur. J. Immunol. 26:142–150.
Arakawa, H., Shimizu, T., and Takeda, S. 1996. Reevaluation of the probabilities for productive rearrangements on the kappa-loci and lambda-loci. Int. Immunol. 8:91–99.
Picard, D., and Schaffner, W. 1984. A lymphocyte-specific enhancer in the mouse immunoglobulin kappa gene. Nature 307:80–82.
Banerji, J., Olson, L., and Schaffner, W. 1983. A lymphocyte specific enhancer is located downstream of the joining region in immunoglobulin heavy chain genes. Cell 33:729–740.
Korholz, D., Gerdau, S., Enczmann, J., Zessack, N., and Burdach, S. 1992. Interleukin 6-induced differentiation of a human B cell line into IgM-secreting plasma cells is mediated by c-fos. Eur. J. Immunol. 22:607–610.
Doglio, L., Kim, J. Y., Bozek, G., and Storb, U. 1994. Expression of lambda and kappa genes can occur in all B cells and is initiated around the same pre-B-cell developmental stage. Dev. Immunol. 4:13–26.
Eisenbeis, C. F., Singh, H., and Storb, U. 1993. PU. 1 is a component of a multiprotein complex which binds an essential site in the murine immunoglobulin lambda 2-4 enhancer. Mol. Cell. Biol. 13:6452–6461.
Blomberg, B. B., Rudin, C. M, and Storb, U. 1991. Identification and localization of an enhancer for the human lambda L chain Ig gene complex. J. Immunol. 147:2354–2358.
Boudinot, P., Drapier, A. M., Cazenave, P. A., and Sanchez, P. 1994. Conserved distribution of lambda subtypes from rearranged gene segments to immunoglobulin synthesis in the mouse B cell repertoire. Eur. J. Immunol. 24:2013–2017.
Boudinot, P., Cazenave, P. A., Sanchez, P., Schlissel, M. S., and Morrow, T. 1994. Conserved distribution of lambda subtypes from rearranged gene segments to immunoglobulin synthesis in the mouse B-cell repertoire Ig heavy-chain protein controls B-cell development by regulating germ-line transcription and retargeting V(D)J recombination. Eur. J. Immunol. 153:1645–1657.
Boudinot, P., Rueffjuy, D., Drapier, A. M, Cazenave, P. A., and Sanchez, P. 1995. Various V-J rearrangement efficiencies shape the mouse-lambda B-cell repertoire. Eur. J. Immunol. 25:2499–2505.
Kudo, A., and Melchers, F. 1987. A second gene, VpreB in the lambda 5 locus of the mouse, which appears to be selectively expressed in pre-B lymphocytes. EMBO J. 6:2267–2272.
Kudo, A., Sakaguchi, N., and Melchers, F. 1987. Organization of the murine lg-related lambda 5 gene transcribed selectively in pre-B lymphocytes. EMBO J. 6:103–107.
Tsubata, T., and Reth, M. 1990. The products of pre-B cell-specific genes (lambda 5 and VpreB) and the immunoglobulin mu chain form a complex that is transported onto the cell surface. J. Exp. Med. 172:973–976.
Karasuyama, H., Rolink, A., Shinkai, Y., Young, F., Alt, F. W., and Melchers, F. 1994. The expression of Vpre-B/lambda 5 surrogate light chain in early bone marrow precursor B cells of normal and B cell-deficient mutant mice. Cell 77:133–143.
Sakaguchi, N., and Melchers, F. 1986. Lambda 5, a new light-chain-related locus selectively expressed in pre-B lymphocytes. Nature 324:579–582.
Melchers, F., Karasuyama, H., Haasner, D., Bauer, S., Kudo, A., Sakaguchi, N., Jameson, B., and Rolink, A. 1993. The surrogate light chain in B-cell development. Immunol. Today 14:60–68.
Rolink, A., Karasuyama, H., Haasner, D., Grawunder, U., Martensson, I. L., Kudo, A., and Melchers, F. 1994. Two pathways of B-lymphocyte development in mouse bone marrow and the roles of surrogate L chain in this development. Immunol. Rev. 137:185–201.
Karasuyama, H., Kudo, A., and Melchers, F. 1990. The proteins encoded by the VpreB and lambda 5 pre-B cell-specific genes can associate with each other and with mu heavy chain. J. Exp. Med. 172:969–972.
Jongstra, J., and Misener, V. 1993. Developmental maturation of the B-cell antigen receptor. Immunol. Rev. 132:107–123.
Misener, V., Downey, G. P., and Jongstra, J. 1991. The immunoglobulin light chain related protein lambda 5 is expressed on the surface of mouse pre-B cell lines and can function as a signal transducing molecule. Int. Immunol. 3:1129–1136.
Takemori, T., Mizuguchi, J., Miyazoe, I., Nakanishi, M., Shigemoto, K., Kimoto, H., Shirasawa, T., Maruyama, N., and Taniguchi, M. 1990. Two types of mu chain complexes are expressed during differentiation from pre-B to mature B cells. EMBO J. 9:2493–2500.
Okabe, T., Bauer, S. R., and Kudo, A. 1992. Pre-B lymphocyte-specific transcriptional control of the mouse VpreB gene. Eur. J. Immunol. 22:31–36.
Martensson, I. L., and Melchers, F. 1994. Pre-B cell-specific lambda 5 gene expression due to suppression in non pre-B cells. Int. Immunol. 6:863–872.
Yang, J., Glozak, M. A., and Blomberg, B. B. 1995. Identification and localization of a developmental stage-specific promoter activity from the murine lambda 5 gene. J. Immunol. 155:2498–2514.
Melchers, F., Rolink, A., Grawunder, U., Winkler, T. H., Karasuyama, H., Ghia, P., and Andersson, J. 1995. Positive and negative selection events during B-lymphopoiesis. Curr. Opin. Immunol. 7:214–227.
Kitamura, D., and Rajewsky, K. 1992. Targeted disruption of mu chain membrane exon causes loss of heavy-chain allelic exclusion. Nature 356:154–156.
Loffert, D., Ehlich, A., Muller, W., and Rajewsky, K. 1996. Surrogate light-chain expression is required to establish immunoglobulin heavy-chain allelic exclusion during early B-cell development. Immunity 4:133–144.
Stanhope-Baker, P., Hudson, K. M., Shaffer, A. L., Constantinescu, A., and Schlissel, M. S. 1996. Cell type-specific chromatin structure determines the targeting of V(D)J recombinasc activity in vitro. Cell85:887–897.
Kitamura, D., Kudo, A., Schaal, S., Muller, W., Melchers, F., and Rajewsky, K. 1992. A critical role of lambda 5 protein in B cell development. Cell 69:823–831.
Kitamura, D., Roes, J., Kuhn, R., and Rajewsky, K. 1991. A B cell-deficient mouse by targeted disruption of the membrane exon of the immunoglobulin mu chain gene. Nature 350:423–426.
Roth, P. E., Doglio, L., Manz, J. T., Kim, J. Y., Lo, D., and Storb, U. 1993. Immunoglobulin gamma 2b transgenes inhibit heavy chain gene rearrangement, but cannot promote B cell development. J. Exp. Med. 178:2007–2021.
Rolink, A., Karasuyama, H., Grawunder, U., Haasner, D., Kudo, A., and Melchers, F. 1993. B cell development in mice with a defective lambda 5 gene. Eur. J. Immunol. 23:1284–1288.
Karasuyama, H., Rolink, A., and Melchers, F. 1993. A complex of glycoproteins is associated with VpreB/lambda 5 surrogate light chain on the surface of mu heavy chain-negative early precursor B cell lines. J. Exp. Med. 178:469–478.
Tonegawa, S. 1983. Somatic generation of antibody diversity. Nature 302:575–581.
Roth, D. B., Zhu, C, and Gellert, M. 1993. Characterization of broken DNA molecules associated with V(D)J recombination. Proc. Natl. Acad. Sci. USA 90:10788–10792.
Hendrickson, E. A., Liu, V. F., and Weaver, D. T. 1991. Strand breaks without DNA rearrangement in V(D)J recombination. Mol. Cell. Biol. 11:3155–3162.
Roth, D. B., Nakajima, P. B., Menetski, J. P., Bosma, M. J., and Gellert, M. 1992. V(D)J recombination in mouse thymocytes: Double-strand breaks near T cell receptor delta rearrangement signals. Cell 69:41–53.
Blunt, T., Finnie, N. J., Taccioli, G. E., Smith, G. C., Demengeot, J., Gottlieb, T. M., Mizuta, R., Varghese, A. J., Alt, F. W., Jeggo, P. A., and Jackson, S. P. 1995. Defective DNA-dependent protein-kinase activity is linked to V(D)J recombination and DNA-repair defects associated with the murine scid mutation. Cell 80:813–823.
Aguilera, R. J., Akira, S., Okazaki, K., and Sakano, H. 1987. A pre-B cell nuclear protein that specifically interacts with the immunoglobulin V-J recombination sequences. Cell 51:909–917.
Hesse, J. E., Lieber, M. R., Mizuuchi, K., and Gellert, M. 1989. V(D)J recombination: A functional definition of the joining signals. Genes Dev. 3:1053–1061.
Bender, J., and Kleckner, N. 1992. Tn10 insertion specificity is strongly dependent upon sequences immediately adjacent to the target-site consensus sequence. Proc. Natl. Acad. Sci. USA 89:7996–8000.
Wu, Z., and Chaconas, G. 1992. Flanking host sequences can exert an inhibitory effect on the cleavage step of the in vitro mu DNA strand transfer reaction. J. Biol. Chem. 267:9552–9558.
Gerstein, R. M., and Lieber, M. R. 1993. Coding end sequence can markedly affect the initiation of V(D)J recombination. Genes Dev. 7:1459–1469.
Boubnov, N. V., Wills, Z. P., and Weaver, D. T. 1995. Coding sequence composition flanking either signal element alters V(D)J recombination efficiency. Nucleic Acids Res. 23:1060–1067.
Lewis, S. M., and Hesse, J. E. 1991. Cutting and closing without recombination in V(D)J joining. EMBO J. 10:3631–3639.
Hagerman, P. J. 1990. Sequence-directed curvature of DNA. Annu. Rev. Biochem. 59:755–781.
Nadeau, J. G., and Crothers, D. M. 1989. Structural basis for DNA bending. Proc. Natl. Acad. Sci. USA 86:2622–2626.
Gerslein, R. M., and Lieber, M. R. 1993. Extent to which homology can constrain coding exon junctional diversity in V(D)J recombination. Nature 363:625–627.
Neuberger, M. S., and Milstein, C. 1995. Somatic hypermutation. Curr. Opin. Immunol. 7:248–254.
Maizels, N. 1995. Somatic hypermutation-How many mechanisms diversify V-region sequences? Cell 83:9–12.
Storb, U. 1996. The molecular basis of somatic hypermutation of immunoglobulin genes. Curr. Opin. Immunol. 8:206–214.
Tomlinson, I. M., Walter, G., Jones, P. T., Dear, P. H., Sonnhammer, E. L. L., and Winter, G. 1996. The imprint of somatic hypermutation on the repertoire of human germline-v genes. J. Mol. Biol. 256:813–817.
Motoyama, N., Okada, H., and Azuma, T. 1991. Somatic mutation in constant regions of mouse lambda 1 light chains. Proc. Natl. Acad. Sci. USA 88:7933–7937.
McKean, D., Huppi, K., Bell, M, Staudt, L., Gerhard, W., and Weigert, M. 1984. Generation of antibody diversity in the immune response of BALB/c mice to influenza virus hemagglutinin. Proc. Natl. Acad. Sci. USA 81:3180–3184.
Jacob, J., Kelsoe, G., Rajewsky, K., and Weiss, U. 1991. Intraclonal generation of antibody mutants in germinal centres. Nature 354:389–392.
Gonzalez Fernandez, A., Gupta, S. K., Pannell, R., Neuberger, M. S., and Milstein, C. 1994. Somaticmutation of immunoglobulin lambda chains: A segment of the major intron hypermutates as much as the complementarity-determining regions. Proc. Natl. Acad. Sci. USA 91:12614–12618.
Betz, A. G., Rada, C., Pannell, R., Milstein, C., and Neuberger, M. S. 1993. Passenger transgenes reveal intrinsic specificity of the antibody hypermutation mechanism: Clustering, polarity, and specific hot spots. Proc. Natl. Acad. Sci. USA 90:2385–2388.
Yelamos, J., Klix, N., Goyenechea, B., Lozano, F., Chui, Y. L., Fernandez, A. G., Pannell, R., Neuberger, M. S., and Milstein, C. 1995. Targeting of non-Lg sequences in place of the V-segment by somatic hypermutation. Nature 376:225–229.
Klein, U., Kueppers, R., and Rajewsky, K. 1994. Variable region gene analysis of B cell subsets derived from a 4-year-old child: Somatically mutated memory B cells accumulate in the peripheral blood already at young age. J. Exp. Med. 180:1383–1393.
Both, G. W., Taylor, L., Pollard, J. W., and Steele, E. J. 1990. Distribution of mutations around rearranged heavy-chain antibody variable-region genes. Mol. Cell. Biol. 10:5187–5196.
Weber, J. S., Berry, J., Litwin, S., and Claflin, J. L. 1991. Somatic hypermutation of the JC intron is markedly reduced in unrearranged kappa and H alleles and is unevenly distributed in rearranged alleles. J. Immunol. 146:3218–3226.
Weber, J. S., Berry, J., Manser, T., and Claflin, J. L. 1991. Position of the rearranged V kappa and its 5’ flanking sequences determines the location of somatic mutations in the J kappa locus. J. Immunol. 146:3652–3655.
Betz, A. G., Milstein, C, Gonzalez Fernandez, A., Pannell, R., Larson, T., and Neuberger, M. S. 1994. Elements regulating somatic hypermutation of an immunoglobulin kappa gene: Critical role for the intron enhancer/matrix attachment region. Cell 77:239–248.
Davis, S. J., Davies, E. A., Barclay, A. N., Daenke, S., Bodine, D., Jones, E. Y., Stuart, D. I., Butters, T. D., Dwek, R. A., and Van-der-Merwe, P. A. 1995. Ligand binding by the immunoglobulin superfamily recognition molecule CD2 is glycosylation-independent. J. Biol. Chem. 270:369–375.
Hengstschlaeger, M., Maizels, N., and Leung, H. 1995. Targeting and regulation of immunoglobulin gene somatic hypermutation and isotype switch recombination. Prog. Nucleic Acid Res. Mol. Biol. 50:67–99.
Peters, A., and Storb, U. 1996. Somatic hypermutation of immunoglobulin genes is linked to transcription initiation. Immunity 4:57–65.
Drapkin, R., Sancar, A., and Reinberg, D. 1994. Where transcription meets repair. Cell 77:9–12.
Mombaerts, P., Iacomini, J., Johnson, R. S., Herrup, K., Tonegawa, S., and Papaioannou, V. E. 1992. RAG-l-deficient mice have no mature B and T lymphocytes. Cell 68:869–877.
Shinkai, Y., Rathbun, C, Lam, K. P., Oltz, E. M., Stewart, V., Mendelsohn, M., Charron, J., Datta, M., Young, F., Stall, A. M., and Alt, F. 1992. RAG-2-deficient mice lack mature lymphocytes owing to inability to initiate V(D)J rearrangement. Cell 68:855–867.
Chun, J. J., Schatz, D. G., Oettinger, M. A., Jaenisch, R., and Baltimore, D. 1991. The recombination activating gene-1 (RAG-1) transcript is present in the murine central nervous system. Cell 64:189–200.
Bernstein, R. M., Schluter, S. F., Lake, D. F., and Marchalonis, J. J. 1994. Evolutionary conservation and molecular-cloning of the recombinase activating gene-1. Biochem. Biophys. Res. Commun. 205:687–692.
Cuomo, C. A., and Oettinger, M. A. 1994. Analysis of regions of RAG-2 important for V(D)J recombination. Nucleic Acids Res. 22:1810–1814.
Sadofsky, M. J., Hesse, J. E., and Gellert, M 1994. Definition of a core region of RAG-2 that is functional in V(D)J recombination. Nucleic Acids Res. 22:1805–1809.
Sadofsky, M. J., Hesse, J. E., McBlane, J. F., and Gellert, M. 1993. Expression and V(D)J recombination activity of mutated RAG-1 proteins. Nucleic Acids Res. 21:5644–5650.
Silver, D. P., Spanopoulou, E., Mulligan, R. C., and Baltimore, D. 1993. Dispensable sequence motifs in the RAG-1 and RAG-2 genes for plasmid V(D)J recombination. Proc. Natl. Acad. Sci. USA 90:6100–6104.
Oettinger, M. A., Schatz, D. G., Gorka, C., and Baltimore, D. 1990. RAG-1 and RAG-2, adjacent genes that synergistically activate V(D)J recombination. Science 248:1517–1523.
Gallo, M. L., Pergola, F., Daniels, G. A., and Lieber, M. R. 1994. Distinct roles for RAG-1 in the initiation of V(D)J recombination and in the resolution of coding ends. J. Biol. Chem. 269:22188–22192.
Schlissel, M., Constantinescu, A., Morrow, T., Baxter, M., and Peng, A. 1993. Double-strand signal sequence breaks in V(D)J recombination are blunt, 5’-phosphorylated, RAG-dependent, and cell cycle regulated. Genes Dev. 7:2520–2532.
Spanopoulou, E., Cortes, P., Shin, C, Huang, C. M., Silver, D. P., Svec, P., and Baltimore, D. 1995. Localization, interaction, and RNA-binding properties of the V(D)J recombination-activating proteins RAG1 and RAG2. Immunity 3:715–726.
Cuomo, C. A., Kirch, S. A., Gyuris, J., Brent, R., and Oettinger, M. A. 1994. Rchl, a protein that specifically interacts with the RAG-1 recombination-activating protein. Proc. Natl. Acad. Sci. USA 91:6156–6160.
Goerlich, D., Prehn, S., Laskey, R. A., and Hartmann, E. 1994. Isolation of a protein that is essential for the first step of nuclear protein import. Cell 79:767–778.
Cortes, P., Ye, Z. S., and Baltimore, D, 1994. RAG-1 interacts with the repeated amino acid motif of the human homologue of the yeast protein SRPI. Proc. Natl. Acad. Sci. USA 91:7633–7637.
Oltz, E. M., Alt, F. W., Lin, W. C., Chen, J., Taccioli, G., Desiderio, S. and Rathbun, G. 1993. A V(D)J recombinase-inducible B-cell line: Role of transcriptional enhancer elements in directing V(D)J recombination. Mol. Cell. Biol. 13:6223–6230.
Chen, J., Shinkai, Y., Young, F., and Alt, F. W. 1994. Probing immune functions in RAG-deficient mice. Curr. Opin. Immunol. 6:313–319.
Leu, T. M. J., and Schatz, D. G. 1995. RAG-1 and RAG-2 are components of a high-molecular-weight complex, and association of RAG-2 with this complex is RAG-1 dependent. Mol. Cell. Biol. 15:5657–5670.
van Gent, D. C, McBlane, J. F., Ramsden, D. A., Sadofsky, M. J., Hesse, J. E., and Gellen, M. 1995. Initiation of V(D)J recombination in a cell-free system. Cell 81:925–934.
Lin, W. C, and Desiderio, S. 1994. Cell cycle regulation of V(D)J recombination-activating protein RAG-2. Proc. Natl. Acad. Sci. USA 91:2733–2737.
Lin, W. C, and Desiderio, S. 1993. Regulation of V(D)J recombination activator protein RAG-2 by phosphorylation. Science 260:953–959.
Verkoczy, L. K., Stiernholm, B. J., and Berinstein, N. L. 1995. Up-regulation of recombination activating gene expression by signal transduction through the surface Ig receptor. J. Immunol. 154:5136–5143.
Wilson, A., Held, W., and MacDonald, H. R. 1994. Two waves of recombinase gene expression in developing fhymocytes. J. Exp. Med. 179:1355–1360.
Li, Y. S., Hayakawa, K., and Hardy, R. R. 1993. The regulated expression of B lineage associated genes during B cell differentiation in bone marrow and fetal liver. J. Exp. Med. 178:951–960.
Stiernholm, N. B., and Berinstein, N. L. 1993. Up-regulated recombination-activating gene expression in slg—variants of a human mature B cell line undergoing secondary Ig lambda rearrangements in cell culture. Eur. J. Immunol. 23:1501–1507.
Billips, L. C., Nunez, C. A., Bertrand, F. E., Stankovic, A. K., Gartiand, G. L., Burrows, P. D., and Cooper, M. D. 1995. Immunoglobulin recombinase gene activity is modulated reciprocally by interleukin-7 and CD 19 in B-cell progenitors. J. Exp. Med. 182:973–982.
Knecht, H., Brousset, P., Bachmann, E., Pallesen, G., and Odermatt, B. F. 1994. Expression of human recombination activating genes (RAG-1 and RAG-2) in lymphoma. Leuk. Lymphoma 15:399–403.
Tsujimoto, Y., Gorham, J., Cossman, J., Jaffe, E., and Croce, C. M. 1985. The t(14;18) chromosome translations involved in B-cell neoplasms result from mistakes in VDJ joining. Science 229:1390–1393.
Showe, L. C, and Croce, C. M. 1987. The role of chromosomal translocations in B-and T-cell neoplasia. Anna. Rev. Immunol. 5:253–277.
Tsujimoto, Y., Jaffe, E., Cossman, J., Gorham, J., Nowell, P. C., and Croce, C. M. 1985. Clustering of breakpoints on chromosome 11 in human B-cell neoplasms with the t(11;14) chromosome translocation. Nature 315:340–343.
Srinivas, S. K., and Sixbey, J. W. 1995. Epstein-Barr-virus induction of recombinase-activating genes RAG1 and RAG2. J. Virol. 69:8155–8158.
Kuhn Hallek, I., Sage, D. R., Stein, L., Groelle, H., and Fingeroth, J. D. 1995. Expression of recombination activating genes (RAG-I and RAG-2) in Epstein-Barr virus-bearing B cells. Blood 85:1289–1299.
Schatz, D. G., Oettinger, M. A., and Baltimore, D. 1989. The V(D)J recombination activating gene, RAG-1. Cell 59:1035–1048.
Schatz, D. G., Oettinger, M. A., and Schlissel, M. S. 1992. V(D)J recombination: Molecular biology and regulation. Annu. Rev. Immunol. 10:359–383.
Tonegawa, S., Sakano, H., Make, R., Traunecker, A., Heinrich, G., Roeder, W., and Kurosawa, Y. 1981. Somatic reorganization of immunoglobulin genes during lymphocyte differentiation. Cold Spring Harbor Symp. Quant. Biol. 45(Pt 2):839–858.
Desiderio, S. V., Yancopoulos, G. D., Paskind, M., Thomas, E., Boss, M. A., Landau, N., Alt, F. W., and Baltimore, D. 1984. Insertion of N regions into heavy-chain genes is correlated with expression of terminal deoxytransfera.se in B cells. Nature 311:752–755.
Bogue, M., Gilfillan, S., Benoist, C., and Mathis, D. 1992. Regulation of N-region diversity in antigen receptors through thymocyte differentiation and thymus ontogeny. Proc. Natl. Acad. Sci. USA 89:11011–11015.
Drexler, H. G., Sperling, C., and Ludwig, W. D. 1993. Terminal deoxynucleotidyl transferase (TdT) expression in acute myeloid leukemia. Leukemia 7:1142–1150.
Bertazzoni, U., and Bollum, F. J. 1982. Terminal Transferase in Immunobiology and Leukemia. New York, Plenum Press.
Kumar, A., Widen, S. G., Williams, K. R., Kedar, P., Karpel, R. L., and Wilson, S. H. 1990. Studies of the domain structure of mammalian DNA polymerase beta. Identification of a discrete template binding domain. J. Biol. Chem. 265:2124–2131.
Matsukage, A., Nishikawa, K., Ooi, T., Seto, Y., and Yamaguchi, M. 1987. Homology between mammalian DNA polymerase beta and terminal deoxynucleotidyltransferase. J. Biol. Chem. 262:8960–8962.
Evans, R. K., and Coleman, M. S. 1989. Photoaffinity labeling of terminal deoxynucleotidyl transferase. 1. Active site directed interactions with 8-azido-2’-deoxyadenosine 5’-triphosphate. Biochemistry 28:707–712.
Yang, B., Gathy, K. N., and Coleman, M. S. 1994. Mutational analysis of residues in the nucleotide binding domain of human terminal deoxynucleotyidyl transferase. J. Biol. Chem. 269:11859–11868.
Feeney, A. J. 1990. Lack of N regions in fetal and neonatal mouse immunoglobulin V-D-J junctional sequences. J. Exp. Med. 172:1377–1390.
Rock, E. P., Sibbald, P. R., Davis, M. M., and Chien, Y. H. 1994. CDR3 length in antigen-specific immune receptors. J. Exp. Med. 179:323–328.
Doyen, N., d’Andon, M. F., Bentolila, L. A., Nguyen, Q. T., and Rougeon, F. 1993. Differential splicing in mouse thymus generates two forms of terminal deoxynucleotidyl transferase. Nucleic Acids Res. 21:1187–1191.
Bentolila, L. A., Fanton, d’A. M., Nguyen, Q. T., Martinez, O., Rougeon, F., and Doyen, N. 1995. The two isoforms of mouse terminal deoxynucleotidyl transferase differ in both the ability to add N regions and subcellular localization. EMBO J. 14:4221–4229.
Smale, S. T., and Baltimore, D. 1989. The “initiator” as a transcription control element. Cell 57:103–113.
Lo, K., Landau, N. R., and Smale, S. T. 1991. LyF-l, a transcriptional regulator that interacts with a novel class of promoters for lymphocyte-specific genes. Mol. Cell. Biol. 11:5229–5243.
Zenzie Gregory, B., O’Shea Greenfield, A., and Smale, S. T. 1992. Similar mechanisms for transcription initiation mediated through a TATA box or an initiator element. J. Biol. Chem. 267:2823–2830.
Ernst, P., Hahm, K., and Smale, S. T. 1993. Both LyF-l and an Ets protein interact with a critical promoter element in the murine terminal transferase gene. Mol. Cell. Biol. 13:2982–2292.
Komori, T., Okada, A., Stewart, V., and Alt, F. W. 1993. Lack of N regions in antigen receptor variable region genes of TdT-deficient lymphocytes. Science 261:1171–1175.
Gilfillan, S., Dierich, A., LeMeur, M., Benoist, C., and Mathis, D. 1993. Mice lacking TdT: Mature animals with an immature lymphocyte repertoire. Science 261:1175–1178.
Gilfillan, S., Benoist, C., and Mathis, D. 1995. Mice lacking terminal deoxynucleotidyl transferase—Adult mice with a fetal antigen receptor repertoire. Immunol. Rev. 148:201–219.
Gilfillan, S., Waltzinger, C., Benoist, C., and Mathis, D. 1994. More efficient positive selection of thymocytes in mice lacking terminal deoxynucleotidyl transferase. Int. Immunol. 6:1681–1686.
Rathmell, W. K., and Chu, G. 1994. A DNA end-binding factor involved in double-strand break repair and V(D)J recombination. Mot. Cell. Biol. 14:4741–4748.
Smider, V., Rathmell, W. K., Lieber, M. R., and Chu, G. 1994. Restoration of X-ray resistance and V(D)J recombination in mutant cells by Ku cDNA. Science 266:288–291.
Weaver, D. T. 1995. What to do at an end: DNA double-strand-break repair. Trends Genet. 11:388–392.
Jeggo, P. A., Taccioli, G. E., and Jackson, S. P. 1995. Menage-a-trois—Double-strand break repair, V(D)J recombination and DNA-PK. Bioessays 17:949–957.
Finnie, N. J., Gottlieb, T. M., Blunt, T., Jeggo, P. A., and Jackson, S. P. 1995. DNA-dependent proteinkinase activity is absent in xrs-6 cells—Implications for site-specific recombination and DNA doublestrand break repair. Proc. Nail. Acad. Sci. USA 92:320–324.
Taccioli, G. E., Gottlieb, T. M., Blunt, T., Priestley, A., Demengeot, J., Mizuta, R., Lehmann, A. R., Alt, F. W., Jackson, S. P., and Jeggo, P. A. 1994. Ku80: Product of the XRCC5 gene and its role in DNA repair and V(D)J recombination. Science 265:1442–1445.
Getts, R. C., and Stamato, T. D. 1994. Absence of a Ku-like DNA end binding activity in the xrs doublestrand DNA repair-deficient mutant. J. Biol. Chem. 269:15981–15984.
Boubnov, N. V., and Weaver, D. T. 1995. SCID cells are deficient in Ku and replication protein A phosphorylation by the DNA-dependent protein kinase. Mol. Cell. Biol. 15:5700–5706.
Kirchgessner, C. U., Patil, C. K., Evans, J. W., Cuomo, C. A., Fried, L. M., Carter, T., Oettinger, M. A., and Brown, J. M. 1995. DNA-dependent kinase (p350) as a candidate gene for the murine SCID defect. Science 267:1178–1183.
Lees Miller, S. P., Godbout, R., Chan, D. W., Weinfeld, M., Day, R. S., 3rd, Barron, G. M., and Allalunis Turner, J. 1995. Absence of p350 subunit of DNA-activated protein kinase from a radiosensitive human cell line. Science 267:1183–1185.
Nussenzweig, A., Chen, C. H., Soares, V. D., Sanchez, M., Sokol, K., Nussenzweig, M. C., and Li, G. C. 1996. Requirement for ku80 in growth and immunoglobulin V(D)J recombination. Nature 382:551–555.
Pleiman, C. M., D’Ambrosio, D., and Cambier, J. C. 1994. The B-cell antigen receptor complex: Structure and signal transduction. Immunol. Today 15:393–399.
Cambier, J. C., Pleiman, C. M., and Clark, M. R. 1994. Signal transduction by the B cell antigen receptor and its coreceptors. Annu. Rev. Immunol. 12:457–486.
Hombach, J., Tsubata, T., Leclercq, L., Stappert, H., and Reth, M. 1990. Molecular components of the B-cell antigen receptor complex of the IgM class. Nature 343:760–762.
Reth, M. 1992. Antigen receptors on B lymphocytes. Annu. Rev. Immunol. 10:97–121.
Hombach, J., Lottspeich, F., and Reth, M. 1990. Identification of the genes encoding the IgM-alpha and Ig-beta components of the IgM antigen receptor complex by amino-terminal sequencing. Eur. J. Immunol. 20:2795–2799.
Yu, L. M., and Chang, T. W. 1992. Human mb-l gene: Complete cDNA sequence and its expression in B cells bearing membrane Ig of various isotypes. J. Immunol. 148:633–637.
Kashiwamura, S., Koyama, T., Matsuo, T., Steinmetz, M., Kimoto, M., and Sakaguchi, N. 1990. Structure of the murine mb-l gene encoding a putative slgM-associated molecule. J. Immunol. 145:337–343.
Hermanson, G. G., Briskin, M., Sigman, D., and Wall, R. 1989. Immunoglobulin enhancer and promoter motifs 5’ of the B29 B-cell-specific gene. Proc. Natl. Acad. Sci. USA 86:7341–7345.
Hashimoto, S., Chiorazzi, N., and Gregersen, P. K. 1994. The complete sequence of the human CD79b (Ig beta/B29) gene: Identification of a conserved exon/intron organization, immunoglobulin-like regulatory regions, and allelic polymorphism. Immunogenetics 40:145–149.
Hashimoto, S., Gregersen, P. K., and Chiorazzi, N. 1993. The human Ig-beta cDNA sequence, a homologue of murine B29, is identical in B cell and plasma cell lines producing all the human Ig isotypes. J. Immunol. 150:491–498.
Friedrich, R. J., Campbell, K. S., and Cambier, J. C. 1993. The gamma subunit of the B cell antigen-receptor complex is a C-terminally truncated product of the B29 gene. J. Immunol. 150:2814–2822.
Kim, K. M., Alber, G., Weiser, P., and Reth, M. 1993. Differential signaling through the Ig-alpha and Ig-beta components of the B cell antigen receptor. Eur. J. Immunol. 23:911–916.
Flaswinkel, H., and Reth, M. 1994. Dual role of the tyrosine activation motif of the Ig-alpha protein during signal transduction via the B cell antigen receptor. EMBO J. 13:83–89.
Gold, M. R., Matsuuchi, L., Kelly, R. B., and DeFranco, A. L. 1991. Tyrosine phosphorylation of components of the B-cell antigen receptors following receptor crosslinking. Proc. Natl. Acad. Sci. USA 88:3436–3440.
Tseng, J., Eisfelder, B. J., and Clark, M. R. 1994. The B-cell antigen receptor complex-Mechanisms and implications of tyrosine kinase activation. Immunol. Res. 13:299–310.
Burkhardt, A. L., Brunswick, M., Bolen, J. B., and Mond, J. J. 1991. Anti-immunoglobulin stimulation of B lymphocytes activates src-related protein-tyrosine kinases. Proc. Nail. Acad. Sci. USA 88:7410–7414.
Yamanashi, Y., Kakiuchi, T., Mizuguchi, J., Yamamoto, T., and Toyoshima, K. 1991. Association of B cell antigen receptor with protein tyrosine kinase Lyn. Science 251:192–194.
Reth, M. 1989. Antigen receptor tail clue. Nature 338:383–384.
Pleiman, C. M., Abrams, C., Gauen, L. T., Bedzyk, W., Jongstra, J., Shaw, A. S., and Cambier, J. C. 1994. Distinct p53/56lyn and p59fyn domains associate with nonphosphorylaled and phosphorylated Ig-alpha. Proc. Nail. Acad. Sci. USA 91:4268–4272.
Clark, M. R., Campbell, K. S., Kazlauskas, A., Johnson, S. A., Hertz, M, Potter, T. A., Pleiman, C, and Cambier, J. C. 1992. The B cell antigen receptor complex: Association of Ig-alpha and Ig-beta with distinct cytoplasmic effectors. Science 258:123–126.
Weiss, A. 1993. Tcell antigen receptor signal transduction: A tale of tails and cytoplasmic protein-tyrosine kinases. Cell 73:209–212.
Clark, M. R., Johnson, S. A., and Cambier, J. C. 1994. Analysis of Ig-alpha-tyrosine kinase interaction reveals two levels of binding specificity and tyrosine phosphorylated Ig-alpha stimulation of Fyn activity. EMBO J. 13:1911–1919.
Saouaf, S. J., Mahajan, S., Rowley, R. B., Kut, S. A., Fargnoli, J., Burkhardt, A. L., Tsukada, S., Witte, O. N., and Bolen, J. B. 1994. Temporal differences in the activation of three classes of non-transmembrane protein tyrosine kinases following B-cell antigen receptor surface engagement. Proc. Natl. Acad. Sci. USA 91:9524–9528.
Nadler, L. M., Anderson, K. C., Marti, G., Bates, M., Park, E., Daley, J. F., and Schlossman, S. F. 1983. B4, a human B lymphocyte-associated antigen expressed on normal, mitogen-activated and malignant B lymphocytes. J. Immunol. 131:244–250.
Stamenkovic, I., and Seed, B. 1988. CD19, the earliest differentiation antigen of the B cell lineage, bears three extracellular immunoglobulin-like domains and an Epstein-Barr virus-related cytoplasmic tail. J. Exp. Med. 168:1205–1210.
Tedder, T. F., and Isaacs, C. M. 1989. Isolation of cDNAs encoding the CD19 antigen of human and mouse B lymphocytes-A new member of the immunoglobulin superfamily. J. Immunol. 143:712–717.
Chalupny, N. J., Aruffo, A., Esselstyn, J. M., Chan, P. Y., Bajorath, J., Blake, J., Gilliland, L. K., Ledbetter, J. A., and Tepper, M. A. 1995. Specific binding of FYN and phosphatidylinositol 3-kinase to the B-cell surface glycoprotein CD 19 through their SRC homology-2 domains. Eur. J. Immunol. 25:2978–2984.
Roifman, C. M., and Ke, S. 1993. CD19 is a substrate of the antigen receptor-associated protein tyrosine kinase in human B cells. Biochem. Biophys. Res. Commun. 194:222–225.
Van Noesel, C. J. M., Lankester, A. C., van Schijndel, G. M. W., and van Lier, R. A. W. 1993. The CR2/CD19 complex on human B cells contains the SRC-family kinase Lyn. Int. Immunol. 5:699–708.
Tuveson, D. A., Carter, R. H., Soltoff, S. P., and Fearon, D. T. 1993. CD19 of B cells as a surrogate kinase insert region to bind phosphatidylinositol 3-kinase. Science 260:986–989.
Carter, R. H., and Fearon, D. T. 1992. CD19: Lowering the threshold for antigen receptor stimulation of B lymphocytes. Science 256:105–107.
Lankester, A. C., van Schijndel, G. M., Rood, P. M., Verhoeven, A. J., and van Lier, R. A. 1994. B cell antigen receptor cross-linking induces tyrosine phosphorylation and membrane translocation of a multi-meric SHC complex that is augmented by CD19 co-ligation. Eur. J. Immunol. 24:2818–2825.
Kehrl, J. H., Riva, A., Wilson, G. L., and Thevenin, C. 1994. Molecular mechanisms regulating CD19, CD20 and CD22 gene expression. Immunol. Today 15:432–436.
Tedder, T. F., Zhou, L. J., and Engel, P. 1994. The CDI9/CD21 signal transduction complex of B lymphocytes. Immunol. Today 15:437–442.
Maloney, M. D., and Lingwood, C. A. 1994. CD19 has a potential CD77 (globotriaosyl ceramide)-binding site with sequence similarity to verotoxin B-subunits: Implications of molecular mimicry for bdB cell adhesion and enterohemorrhagic Escherichia coli pathogenesis. J. Exp. Med. 180:191–201.
Ledbetter, J. A., Rabinovitch, P. S., June, C. H., Song, C. W., Clark, E. A., and Uckun, F. M. 1988. Antigen-independent regulation of cytoplasmic calcium in B cells with a 12-kDa B-cell growth factor and anti-CD19. Proc. Natl. Acad. Sci. USA 85:1897–1901.
Smith, S. H., Rigley, K. P., and Callard, R. E. 1991. Activation of human B cells through the CD 19 surface antigen results in homotypic adhesion by LFA-I dependent and independent mechanisms. Immunology 73:293–301.
Callard, R. E., Rigley, K. P., Smith, S. H., Thurstan, S., and Shields, J. G. 1992. CD19 regulation of human B cell responses. B cell proliferation and antibody secretion are inhibited or enhanced by ligation of the CD19 surface glycoprotein depending on the stimulating signal used. J. Immunol. 148:2983–2987.
DeRie, M. A., Schumacher, T. N. M., van Schijndel, G. M. W., van Lier, R. A. W., and Miedema, F. 1989. Regulatory role of CD19 molecules in B cell activation and differentiation. Cell. Immunol. 118:368–381.
Rigley, K. P., and Callard, R. E. 1991. Inhibition of B cell proliferation with anti-CD19 monoclonal antibodies: Anti-CD 19 antibodies do not interfere with early signaling events triggered by anti-IgM or interleukin 4. Eur. J. Immunol. 21:535–540.
Schraven, B., Ratnofsky, S., Gaumont, Y., Lindegger, H., Kirchgessner, H., Bruyns, E., Moebius, U., and Meuer, S. C. 1994. Identification of a novel dimeric phosphoprotein (PP29/30) associated with signaling receptors in human T lymphocytes and natural killer cells. J. Exp. Med. 180:897–906.
Pezzutto, A., Dorken, B., Rabinovitch, P., Ledbetter, J., Moldenhauer, G., and Clark, E. 1987. CD19 monoclonal antibody HD37 inhibits anti-immunoglobulin induced B-cell activation and proliferation. J. Immunol. 138:2793–2799.
Uckun, F. M., Jaszcz, W., Ambrus, J. L., Fauci, A. S., Gajl Peczalska, K., Song, C. W., Wick, M. R., Myers, D.E., Waddick, K., and Ledbetter, J. A. 1988. Detailed studies on expression and function of CD19 surface determinant by using B43 monoclonal antibody and clinical potential of anti-CD 19 immunotoxins. Blood 71:13–29.
Uckun, F. M., and Ledbetter, J. A. 1988. Immunobiologic differences between normal and leukemic human B-cell precursors. Proc. Natl. Acad. Sci. USA 85:8603–8607.
Carter, R. H., Tuveson, D. A., Park, D. J., Rhee, S. G., and Fearon, D. T. 1991. The CD19 complex of B lymphocytes: Activation of phospholipase C by a protein tyrosine kinase-dependent pathway that can be enhanced by the membrane IgM complex. J. Immunol. 147:3663–3671.
Chaouchi, N., Vazquez, A., Galanaud, P., and Leprince, C. 1995. B-cell antigen receptor-mediated apoptosis-Importance of accessory molecules CD19 and CD22, and of surface IgM cross-linking. J. Immunol. 154:3096–3104.
Tedder, T. F., and Engel, P. 1994. CD20-A regulator of cell-cycle progression of B-lymphocytes. Immunol. Today 15:450–454.
Tedder, T. F., Klejman, G., Disteche, C. M., Adler, D. A., Schlossman, S. F., and Saito, H. 1988. Cloning of a complementary DNA encoding a new mouse B lymphocyte differentiation antigen, homologous to the human Bl (CD20) antigen, and localization of the gene to chromosome 19. J. Immunol. 141:4388–4394.
Tedder, T. F., Disteche, C. M., Louie, E., Adler, D. A., Croce, C. M., Schlossman, S. F., and Saito, H. 1989. The gene that encodes the human CD20 (B1) differentiation antigen is located on chromosome 11 near the T(Il:I4)(ql3;q32) translocation site. J.Immunol. 142:2555–2559.
Bubien, J. K., Zhou, L. J., Bell, P. D., Frizzell, R. A., and Tedder, T. F.1993. Transfection of the CD20 cell surface molecule into ectopic cell types generates a Ca2+ conductance found constitutively in B lymphocytes. J. Celt Biol. 121:1121–1132.
Hupp, K., Siwarski, D., Mock, B. A., and Kinet, J. P. 1989. Gene mapping of the three subunits of the high affinity FcR for IgE to mouse chromosomes 1 and 19. J. Immunol. 143:3787–3791.
Stashenko, P., Nadler, L. M., Hardy, R., and Schlossman, S. F. 1981. Expression of cell surface markers after human B lymphocyte activation. Proc. Natl. Acad. Sci. USA 176:1543–1550.
Clark, E. A., and Ledbetter, J. A. 1986. Activation of human B cell proliferation through surface Bp35 and Bp50. Proc. Nail. Acad Sci. USA 83:4494–4498.
Golay, J. T., Clark, E. A., and Beverley, P. C. 1985. The CD20 (Bp35) antigen is involved in activation of B cells from the G0 to the G1 phase of the cell cycle. J. Immunol. 135:3795–3801.
Tedder, T. F., and Schlossman, S. F. 1988. Phosphorylation of the (BHCD20) molecule by normal and malignant human B lymphocytes. J. Biol. Chem. 263:10009–10015.
Deans, J. P., Schieven, G. L., Shu, G. L., Valentine, M. A., Gilliland, L. A., Aruffo, A., Clark, E. A., and Ledbetter, J. A. 1993. Association of tyrosine and serine kinases with the B cell surface antigen CD20. Induction via CD20 of tyrosine phosphorylation and activation of phospholipase C-gamma 1 and PLC phospholipase C-gamma 2. J. Immunol. 151:4494–4504.
Zola, H. 1987. The surface antigens of human B lymphocytes. Immunol. Today 8:308–315.
Kanzaki, M., Shibata, H., Mogami, H., and Kojima, I. 1995. Expression of calcium-permeable cation channel CD20 accelerates progression through the g(l) phase in Balb/c 3T3 cells. J. Bitil. Chem. 270:13099–13104.
Deans, J. P., Kalt, L., Ledbetter, J. A., Schieven, G. L., Bolen, J. B., and Johnson, P. 1995. Association of 75/80-kDa phosphoproteins and the tyrosine kinases LYN, FYN, and LCK with the B-cell molecule-CD20-Evidence against involvement of the cytoplasmic regions of CD20. J. Biol. Chem. 270:22632–22638.
Rosenthal, P., Rimm, I. J., Umiel, T., Griffin, J. D., Osathanondh, R., Schlossman, S. F., and Nadler, L. M, 1983. Ontogeny of human hematopoietic cells: Analysis utilizing monoclonal antibodies. J. Immunol. 131:232–237.
Holder, M., Grafton, G., Macdonald, L., Finney, M., and Gordon, J. 1995. Engagement of CD20 suppresses apoptosis in germinal center B-cells. Eur. J. Immunol. 25:3160–3164.
Valentine, M. A., Cotner, T., Gaur, L., Torres, R., and Clark, E. A. 1987. Expression of the human B-cell surface protein CD20-. Alteration by phorbol 12-myristate 13-acetate. Prix: Nail. Acad. Sci. USA 84:8085–8089.
Himmelmann, A., Wilson, G. L., Lucas, B., Thevenin, C., and Kehrl, J. 1996. B-cell and developmental stage-specific expression of the human CD20 gene is achieved via a novel pu.l/pip site. J. Invest. Med. 44:A237.
Law, C. L., Sidorenko, S. P., and Clark, E. A. 1994. Regulation of lymphocyte-activation by the cell-surface molecule CD22. Immunol. Today 15:442–449.
Wilson, G. L., Fox, C. H., Fauci, A. S., and Kehrl, J. H. 1991. cDNA cloning of the B cell membrane protein CD22: A mediator of B-B cell interactions. J. Exp. Med. 173:137–148.
Slamenkovic, J., and Seed, B. 1990. The B cell antigen CD22 mediates monocyle and erythrocyte adhesion. Nature 345:74–77.
Engel, P., Nojima, Y., Rothstein, D., Zhou, L. J., Wilson, G. L., Kehrl, J. H., and Tedder, T. F.1993. The same epitope on CD22 of B lymphocytes mediates the adhesion of erythrocytes, T and B lymphocytes, neutrophils, and monocytes. J. Immunol. 150:4719–4732.
Sgroi, D., Koretzky, G. A., and Stamenkovic, I. 1995. Regulation of CD45 engagement by the B-cell receptor CD22. Proc. Natl. Acad. Sci. USA 92:4026–4030.
Powell, L. D., Sgroi, D., Sjoberg, E. R., Stamenkovic, I., and Varki, A. 1993. Natural ligands of the B cell adhesion molecule CD22(3 carry N-linked oligosaccharides with a-2,6-linkcd sialic acids that arc required for recognition. J. Biol. Chem. 268:7019–7027.
Schulte, R. J., Campbell, M. A., Fischer, W. H., and Sefton, B. M. 1992. Tyrosine phosphorylation of CD22 during B-cell activation. Science 258:1001–1004.
Leprince, C., Draves, K. E., Geahlen, R. L., Ledbetter, J. A., and Clark, E. A. 1993. CD22 associates with the human surface IgM-B-cell antigen receptor complex. Proc. Nail. Acad. Sci. USA 90:3236–3240.
Peaker, C. J., and Neuberger, M. S. 1993. Association of CD22 with the B cell antigen receptor. Eur. J. Immunol. 23:1358–1366.
Pezzutto, A., Rabinovitch, P. S., Dorken, B., Moldenhauer, G., and Clark, E. A. 1988. Role of the CD22 human B cell antigen in B cell triggering by anti-immunoglobulin. J. Immunol. 140:1791–1795.
Varki, A. 1992. Selectins and other mammalian sialic acid-binding lectins. Curr. Opin. Cell Biol. 4:257–261.
Sgroi, D., Varki, A., Braesch Andersen, S., and Stamenkovic, I. 1993. CD22, a B cell-specific immunoglobulin superfamily member, is a sialic acid-binding lectin. J. Biol. Chem. 268:7011–7018.
Clark, E. A. 1993. CD22, a B cell-specific receptor, mediates adhesion and signal transduction. J. Immunol. 150:4715–4718.
Campbell, M. A., and Klinman, N. R. 1995. Phosphotyrosine-dependent association between CD22 and protein-tyrosine-phosphatase 1c. Eur. J. Immunol. 25:1573–1579.
Doody, G. M., Justement, L. B., Delibrias, C. C., Matthews, R. J., Lin, J. J., Thomas, M. L., and Fearon, D. T. 1995. A role in B-cell activation for CD22 and the protein-tyrosine-phosphatase SHP. Science 269:242–244.
Doody, G., Justement, L., Matthews, R. J., Roy, G., Lin, J., Thomas, M., and Fearon, D. 1995. Tyrosine phosphorylation of CD22 by membrane immunoglobulin recruits the negative regulatory protein-tyrosinephosphatase, SHPTPI. EASEB J. 9:A505.
Stamenkovic, I., Sgroi, D., Aruffo, A., Sy, M. S., and Anderson, T. 1991. The B lymphocyte adhesion molecule CD22 interacts with leukocyte common antigen CD45RO on T cells and alpha 2-6 sialyltransferase, CD75, on B cells. Cell 66:1133–1144.
Sgroi, D., and Stamenkovic, I. 1994. The B-cell adhesion molecule CD22 is cross-species reactive and recognizes distinct sialoglycoproteins on different functional T-cell subpopulations. Scand. J. Immunol. 39:433–438.
Tuscano, J., Engel, P., Tedder, T. F., and Kehrl, J. H. 1996. Engagement of the adhesion receptor CD22 triggers a potent stimulatory signal for B-cells and blocking CD22/CD221 interactions impairs T-cell proliferation. Blood 87:4723–4730.
Law, C. L., Aruffo, A., Chandran, K. A., Doty, R. T., and Clark, E. A. 1995. Ig domain-1 and domain-2 of murine CD22 constitute the ligand binding domain and bind multiple sialylated ligands expressed on B-cells and T-cells. J. Immunol. 155:3368–3376.
Aruffo, A., Kanner, S. B., Sgroi, D., Ledbetter, J. A., and Stamenkovic, I. 1992. CD22-mediated stimulation of T cells regulates T-cell receptor/CD3-induced signaling. Proc. Natl. Acad. Sci. USA 89:10242–10246.
Thomas, M. L. 1989. The leukocyte common antigen family. Annu. Rev. Immunol. 7:339–369.
Poppema, S., Lai, R., Visser, L., and Yan, X. J. 1996. CD45 (leukocyte common antigen) expression in T-lymphocyte and B-lymphocyte subsets. Leuk. Lymphoma 20:217–222.
Justement, L. B., Campbell, K. S., Chien, N. C., and Cambier, J. C. 1991. Regulation of B cell antigen receptor signal transduction and phosphorylation by CD45. Science 252:1839–1842.
Reth, M. 1995. The B-cell antigen receptor complex and co-receptors. Immunol. Today 16:310–313.
Koretzky, G. A., Picus, J., Schultz, T., and Weiss, A. 1991. Tyrosine phosphatase CD45 is required for T cell antigen receptor and CD2 mediated activation of a protein tyrosine kinase and interkeukin 2 production. Proc. Noll. Acad. Sci. USA 88:2037–2041.
Hovis, R. R., Donovan, J. A., Musci, M. A., Motto, D. G., Goldman, F. D., Ross, S. E., and Koretzky, G. A. 1993. Rescue of signaling by a chimeric protein containing the cytoplasmic domain of CD45. Science 260:544–546.
Hurley, T. R., Hyman, R., and Sefton, B. M. 1993. Differential effects of expression of the CD45 tyrosine protein phosphatase on the tyrosine phosphorylation of the LCK, FYN, and c-SRC tyrosine protein kinases. Mol. Cell. Biol. 13:1651–1656.
McFarland, E. D., Hurley, T. R., Pingel, J. T., Sefton, B. M., Shaw, A., and Thomas, M. L. 1993. Correlation between SRC family member regulation by the protein-tyrosine-phosphatase CD45 and trans-membrane signaling through the T-cell receptor. Proc. Natl. Acad. Sci. USA 90:1402–1406.
Koretzky, G. A. 1993. Role of the CD45 tyrosine phosphatase in signal transduction in the immune system. FASEB J. 7:420–426.
Sieh, M., Bolen, J. B., and Weiss, A. 1993. CD45 specifically modulates binding of LCK to a phosphopeptide encompassing the negative regulatory tyrosine of LCK. EMBO J. 12:315–321.
Shiroo, M., Goff, L., Biffen, M., Shivnan, E., and Alexander, D. 1992. CD45 tyrosine phosphatase-activated P59FYN couples the T cell antigen receptor to pathways of diacylglycerol production, protein kinase C activation and calcium influx. EMBO J. 11:4887–4897.
Lin, J., Brown, V. K., and Justement, L. B.1992. Regulation of basal tyrosine phosphorylation of the B cell antigen receptor complex by the protein tyrosine phosphatase, CD45. J. Immunol. 149:3182–3190.
Kishihara, K., Penninger, J., Wallace, V. A., Kundig, T. M., Kawai, K., Wakeham, A., Timms, E., Pfeffer, K., Ohashi, P. S., Thomas, M. L., Furlonger, C., Paige, C. J., and Mak, T. W. 1993. Normal B lymphocyte development but impaired T cell maturation in CD45-exon 6 protein tyrosine phosphatase-deficient mice. Cell 74:143–156.
Cyster, J. G., Healy, J. I., Kishihara, K., Mak, T. W., Thomas, M. L., and Goodnow, C. C. 1996. Regulation of B-lymphocyte negative and positive selection by tyrosine phosphatase CD45. Nature 381:325–328.
Gold, M. R., Law, D. A., and DeFranco, A. L. 1990. Stimulation of protein tyrosine phosphorylation by the B-lymphocyte antigen receptor. Nature 345:810–813.
Reth, M. 1994. B cell antigen receptors. Curr. Opin. Immunol. 6:3–8.
Sillman, A. L., and Monroe, J. G. 1995. Association of p72(syk) with the sre homology-2 (SH2) domains of PLC-gamma-1 in B-lymphocytes. J. Biol Chem. 270:11806–11811.
Klaus, G. G., Harnett, M. M., and Rigley, K. P. 1989. G-protein regulation of polyphosphoinositide breakdown in B cells. Adv. Exp. Med. Biol. 254:95–100.
Coggeshall, K. M., McHugh, J. C., and Altman, A. 1992. Predominant expression and activation-induced tyrosine phosphorylation of phospholipase C-gamma 2 in B lymphocytes. Proc. Natl. Acad. Sci. USA 89:5660–5664.
Sillman, A. L., and Monroe, J. G. 1994. Surface IgM-stimulated proliferation, inositol phospholipid hydrolysis, Ca2 +, and tyrosine phosphorylation are not altered in B-cells from p59 (fyn-/-) mice. J. Leukoc. Biol. 56:812–816.
Sanchez, M., Misulovin, Z., Burkhardt, A. L., Mahajan, S., Costa, T., Franke, R., Bolen, J. B., and Nussenzweig, M. 1993. Signal transduction by immunoglobulin is mediated through Ig alpha and Ig beta. J. Exp. Med. 178:1049–1055.
Harnett, M. M., Holman, M. J., and Klaus, G. G. 1989. Regulation of surface IgM-and IgD-mediated inositol phosphate formation and Ca2* mobilization in murine B lymphocytes. Eur. J. Immunol. 19:1933–1939.
Campbell, M. A., and Sefton, B. M. 1990. Protein tyrosine phosphorylation is induced in murine B lymphocytes in response to stimulation with anti-immunoglobulin. EMBO J. 9:2125–2131.
Brunswick, M., Samelson, L. E., and Mond, J. J. 1991. Surface immunoglobulin crosslinking activates a tyrosine kinase pathway in B cells that is independent of protein kinase C. Proc. Natl. Acad. Sci. USA 88:1311–1314.
Dymecki, S. M., Zwollo, P., Zeller, K., Kuhajda, F. P., and Desiderio, S. V. 1992. Structure and developmental regulation of the B-lymphoid tyrosine gene blk. J. Biol. Chem. 267:4815–4823.
Nagai, K., Takala, M., Yamamura, H., and Kurosakiso, T. 1995. Tyrosine phosphorylation of SHC is mediated through lyn and syk in B-cell receptor signaling. J. Biol. Chem. 270:6824–6829.
Pawson, T., and Gish, G. D. 1992. SH2 and SH3 domains: From structure to function. Cell 71:359–362.
Prasad, K. V., Janssen, O., Kapeller, R., Raab, M., Cantley, L. C., and Rudd, C. E. 1993. Src-homology 3 domain of protein kinase p59fyn mediates binding to phosphatidylinositol 3-kinase in T cells. Proc. Nail. Acad. Sci. USA 90:7366–7370.
Liu, X., Marengere, L. E., Koch, C. A., and Pawson, T. 1993. The v-src SH3 domain binds phosphatidylinositol 3’-kinase. Mol. Cell. Biol. 13:5225–5232.
Vogel, L. B., and Fujita, D. J. 1993. The SH3 domain of p56lck is involved in binding to phosphatidylinositol 3’-kinase from T lymphocytes. Mol. Cell. Biol. 13:7408–7417.
Bergman, M., Mustelin, T., Oetken, C., Partanen, J., Flint, N. A., Amrein, K. E., Autero, M., Bum, P., and Alitalo, K. 1992. The human p50csk tyrosine kinase phosphorylates p56lck at Tyr-505 and down regulates its catalytic activity. EMBO J. 11:2919–2924.
Nada, S., Okada, M., MacAuley, A., Cooper, J. A., and Nakagawa, H. 1991. Cloning of a complementary DNA for a protein-tyrosine kinase that specifically phosphorylates a negative regulatory site of p60c-src. Nature 351:69–72.
Okada, M., and Nakagawa, H. 1989. A protein tyrosine kinase involved in regulation of pp60c-src function. J. Biol. Chem. 264:20886–20893.
Kong, G. H., Bu, J. Y., Kurosaki, T., Shaw, A. S., and Chan, A. C. 1995. Reconstitution of Syk function by the ZAP-70 protein tyrosine kinase. Immunity 2:485–492.
Kurosaki, T., Takata, M., Yamanashi, Y., Inazu, T., Taniguchi, T., Yamamoto, T., and Yamamura, H. 1994. Syk activation by the Src-family tyrosine kinase in the B cell receptor signaling. J. Exp. Med. 179:1725–1729.
Iwashima, M., Irving, B. A., Van Oers, N. S., Chan, A. C., and Weiss, A. 1994. Sequential interactions of the TCR with two distinct cytoplasmic tyrosine kinases. Science 263:1136–1139.
Kurosaki, T., Johnson, S. A., Pao, L., Sada, K., Yamamura, H., and Cambier, J. C. 1995. Role of the syk autophosphorylation site and SH2 domains in B-cell antigen receptor signaling. J. Exp. Med. 182:1815–1823.
Hata, A., Sabe, H., Kurosaki, T., Takata, M., and Hanafusa, H. 1994. Functional analysis of csk in signaltransduction through the B-cell antigen receptor. Mol. Cell. Biol. 14:7306–7313.
Panchamoorthy, G., Fukazawa, T., Miyake, S., Soltoff, S., Reedquist, K., Druker, B., Shoelson, S., Cantley, L., and Band, H. 1996. P120(cbl) is a major substrate of tyrosine phosphorylation upon B-cell antigen receptor stimulation and interacts in-vivo with fyn and syk tyrosine kinases, grb2 and SHC adapters, and the p85 subunit of phosphatidylinositol 3-kinase. J. Biol. Chem. 271:3187–3194.
Desiderio, S. 1993. Human genetics. Becoming B cells. Nature 361:202–203.
Aoki, Y., Isselbacher, K. J., and Pillai, S. 1994. Bruton tyrosine kinase is tyrosine phosphorylated and activated in pre-B lymphocytes and receptor-ligated B cells. Proc. Natl. Acad. Sci. USA 91:10606–10609.
de Weers, M., Brouns, G. S., Hinshelwood, S., Kinnon, C., Schuurman, R. K., Hendriks, R. W., and Borst, J. 1994. B-cell antigen receptor stimulation activates the human Bruton’s tyrosine kinase, which is deficient in X-linked agammaglobulinemia. J. Biol. Chem. 269:23857–23860.
Tsukada, S., Saffran, D. C., Rawlings, D. J., Parolini, O., Allen, R. C., Klisak, L., Sparkes, R. S., Kubagawa, H., Mohandas, T., Quan, S., Belmont, J., Cooper, M. D., Conley, M. E., and Witte, O. N. 1993. Deficient expression of a B cell cytoplasmic tyrosine kinase in human X-linked agammaglobulinemia. Cell 72:279–290.
Li, T. J., Tsukada, S., Satterthwaite, A., Havlik, M. H., Park, H., Takatsu, K., and Witte, O. N. 1995. Activation of Bruton’s tyrosine kinase (btk) by a point mutation in its pleckstrin homology (PH) domain. Immunity 2:451–460.
Bolen, J. B. 1993. Nonreceptor tyrosine protein kinases. Oncogene 8:2025–2031.
Vetrie, D., Vorechovsky, I., Sideras, P., Holland, J., Davies, A., Flinter, F., Hammarstroem, L., Kinnon, C, Levinsky, R., Bobrow, M., Smith, E., and Bentley, D. R. 1993. The gene involved in X-linked agammaglobulinaemia is a member of the src family of protein-tyrosine kinases. Nature 361:226–233.
Rawlings, D. J., Saffran, D. C., Tsukada, S., Largaespada, D. A., Grimaldi, J. C., Cohen, L., Mohr, R. N., Bazan, J. F., Howard, M., and Copeland, N. G. 1993. Mutation of unique region of Bruton’s tyrosine kinase in immunodeficient XID mice. Science 261:358–361.
Thomas, J. D., Sideras, P., Smith, C. I., Vorechovsky, I., Chapman, V., and Paul, W. E. 1993. Colocalization of X-linked agammaglobulinemia and X-linked immunodeficiency genes. Science 261:355–358.
Rawlings, D. J., Scharenberg, A. M., Park, H., Wahl, M. I., Lin, S. Q., Kato, R. M., Fluckiger, A. C, Witte, O. N., and Kinet, J. P. 1996. Activation of BTK by a phosphorylation mechanism initiated by src family kinases. Science 271:822–825.
Pei, D. H., Wang, J., and Walsh, C. T. 1996. Differential functions of the 2 src homology-2 domains in protein-tyrosine-phosphatase SH-PTP1. Proc. Nail. Acad. Sci. USA 93:1141–1145.
Eck, M. J., Pluskey, S., Trub, T., Harrison, S. C., and Shoelson, S. E. 1996. Spatial constraints on the recognition of phosphoproteins by the tandem sh2 domains of the phosphatase sh-ptp2. Nature 379:277–280.
Pani, G., Kozlowski, M., Cambier, J. C., Mills, G. B., and Siminovitch, K. A. 1995. Identification of the tyrosine phosphatase PTP1C as a B cell antigen receptor-associated protein involved in the regulation of B cell signaling. J. Exp. Med, 181:2077–2084.
Kozlowski, M., Pani, G., Pawson, T., and Siminovitch, K. A. 1996. The tyrosine phosphatase PTPlc associates with VAV, GRB2, and mSOSl in hematopoietic cells. J. Biol. Chem. 271:3856–3862.
Wu, Y. J., Pani, G., Siminovitch, K. A., and Hozumi, N. 1995. Antigen receptor-triggered apoptosis in immature B-cell lines is associated with the binding of a 44-kDa phosphoprotein to the ptplc tyrosine phosphatase. Eur. J. Immunol. 25:2279–2284.
Cyster, J. G., and Goodnow, C. C. 1995. Protein tyrosine phosphatase 1C negatively regulates antigen receptor signaling in B lymphocytes and determines thresholds for negative selection. Immunity 2:13–24.
Bignon, J. S., and Siminovitch, K. A. 1994. Identification of ptplc mutation as the genetic defect in motheaten and viable moth-eaten mice-A step toward defining the roles of protein-tyrosine phosphatases in the regulation of hematopoietic-cell differentiation and function. C/w. Immunol. Immunopathol. 73:168–179.
Tsui, H. W., Siminovitch, K. A., de Souza, L., and Tsui, F. W. 1993. Motheaten and viable motheaten mice have mutations in the haematopoietic cell phosphatase gene. Nat. Genet. 4:124–129.
Yu, C. C. K., Tsui, H. W., Ngan, B. Y., Shulman, M. J., Wu, G. E., and Tsui, F. W. L. 1996. B-cells and T-cells are not required for the viable moth-eaten phenotype. J. Exp. Med. 183:371–380.
Conley, M. E., and Delacroix, D. L. 1987. Intravascular and mucosal immunoglobulin A: Two separate but related systems of immune defense? Ann. Intern. Med. 106:892–899.
Brandtzaeg, P. 1995. Molecular and cellular aspects of the secretory immunoglobulin system. APMIS 103:1–19.
Lamm, M. E., Nedrud, J. G., Kaetzel, C. S., and Mazanec, M. B. 1995. IgA and mucosal defense. APMIS 103:241–246.
Lamm, M. E. 1988. The IgA mucosal immune system. Am. J. Kidney Dis. 12:384–387.
Mestecky, J. 1988. Immunobiology of IgA. Am. J. Kidney Dis. 12:378–383.
Kramer, D. R., and Cebra, J. J. 1995. Early appearance of “natural” mucosal IgA responses and germinal centers in suckling mice developing in the absence of maternal antibodies. J. Immunol. 154:2051–2062.
Kramer, D. R., and Cebra, J. J. 1994. Modulation of the neonatal IgA response to enteric antigens by maternal antibody. Adv. Exp. Med. Biol. 355:271–275.
Flores, A. E., Nelson, J. A., Wu, X. Y., and Ferrieri, P. 1993. Antibody profiles to the group B streptococcal beta antigen in maternal and infant paired sera. APMIS 101:41–49.
Hanson, L. A., Adlerberth, I., Carlsson, B., Zaman, S., Hahn Zoric, M., and Jalil, F. 1990. Antibody-mediated immunity in the neonate. Paediatr. Paedol. 25:371–376.
Kramer, D. R., and Cebra, J. J. 1995. Role of maternal antibody in the induction of virus-specific and bystander IgA responses in Peyers patches of suckling mice. Int. Immunol. 7:911–918.
MacDonald, G. C. 1983. The ontogeny of the mucosal immune system in rodents. In: Parrott, D., and MacDonald, G. C., eds., The Ontogeny of the Immune System of the Gut, Boca Raton, CRC Press, p. 51.
Truedsson, L., Baskin, B., Pan, Q., Rabbani, H., Vorechovsky, I., Smith, C. I. E., and Hammarstrom, L. 1995. Genetics of IgA deficiency. APMIS 103:833–842.
Mostov, K. E., and Cardone, M. H. 1995. Regulation of protein traffic in polarized epithelial cells. Bioessays 17:129–138.
Song, W., Apodaca, G., and Mostov, K. 1994. Transcytosis of the polymeric immunoglobulin receptor is regulated in multiple intracellular compartments. J. Biol. Chem. 269:29474–29480.
Mostov, K. E. 1994. Transepithelial transport of immunoglobulins. Annu. Rev. Immunol. 12:63–84.
Song, W., Bomsel, M., Casanova, J., Vaerman, J. P., and Mostov, K. 1994. Stimulation of transcytosis of the polymeric immunoglobulin receptor by dimeric IgA. Proc. Natl. Acad. Sci. USA 91:163–166.
Song, W., Vaerman, J. P., and Mostov, K. E. 1995. Dimeric and tetrameric IgA are transcytosed equally by the polymeric Ig receptor. J. Immunol. 155:715–721.
Chapin, S. J., Enrich, C., Aroeti, B., Havel, R. J., and Mostov, K. E. 1996. Calmodulin binds to the basolateral targeting signal of the polymeric immunoglobulin receptor. J. Biol. Chem. 271:1336–1342.
Casanova, J. E., Breitfeld, P. P., Ross, S. A., and Mostov, K. E. 1990. Phosphorylation of the polymeric immunoglobulin receptor required for its efficient transcytosis. Science 248:742–745.
Apodaca, G., and Mostov, K. E. 1993. Transcytosis of placental alkaline phosphatase-polymeric immunoglobulin receptor fusion proteins is regulated by mutations of Ser664. J. Biol. Chem. 268:23712–23719.
Mestecky, J., Russell, M. W., Jackson, S., and Brown, T. A. 1986. The human IgA system: A reassessment. Clin. Immunol. Immunopothol. 40:105–114.
Mestecky, J., and McGhee, J. R. 1987. Immunoglobulin A (IgA): Molecular and cellular interactions involved in IgA biosynthesis and immune response. Adv. Immunol. 40:153–245.
Hiki, Y., Iwase, H., Saitoh, M., Saitoh, Y., Horii, A., Hotta, K., and Kobayashi, Y. 1996. Reactivity of glomerular and serum IgAl to jacalin in IgA nephropathy. Nephron 72:429–435.
Mestecky, J., and Russell, M. W. 1986. IgA subclasses. Monogr. Allergy 19:277–301.
Qiu, J. Z., Brackee, G. P., Plaut, A. G., Sneller, M. C., and Strober, W. 1986. Analysis of the specificity of bacterial immunoglobulin-A (IgA) proteases by a comparative study of APE serum IgAs as substrates. Infect. Immun. 64:933–937.
de Lange, G. G. 1989. Polymorphisms of human immunoglobulins: Gm, Am, Em and Km allotypes. Exp. Clin. Immunogenet. 6:7–17.
Butor, C., Couedelcourteille, A., Venet, A., and Guillet, J. G. 1995. Local immunity and vaccination. Med. Sci. 11:703–711.
Mombaerts, P., Mizoguchi, E., Grusby, M. J., Glimcher, L. H., Bhan, A. K., and Tonegawa, S. 1993. Spontaneous development of inflammatory bowel disease in T cell receptor mutant mice. Cell 75:274–282.
Sadlack, B., Merz, H., Schorle, H., Schimpl, A., Feller, A. C., and Horak, L. 1993. Ulcerative colitis-like disease in mice with a disrupted interleukin-2 gene. Cell 75:253–261.
Lehner, T., Bergmeier, L. A., Tao, L., Panagiotidi, C., Klavinskis, L. S., Hussain, L., Ward, R. G., Meyers, N., Adams, S. E., Gearing, A. J., and Brookes, R. 1994. Targeted lymph node immunization with simian immunodeficiency virus p27 antigen to elicit genital, rectal, and urinary immune responses in nonhuman primates. J. Immunol. 153:1858–1868.
Kiyono, H., Miller, C. J., Lu, Y. C., Lehner, T., Cranage, M., Huang, Y. T., Kawabata, S., Marthas, M., Roberts, B., Nedrud, J. G., Lamm, M. E., Bergmeier, L., Brookes, R., Tao, L., and McGhee, J. R. The common mucosal immune system for the reproductive tract-Basic principles applied toward an AIDS vaccine. Adv. Drug Delh: Rev. 18:23–52.
Bukawa, H., Sekigawa, K. I., Hamajima, K., Fukushima, J., Yamada, Y., Kiyono, H., and Okuda, K. 1995. Neutralization of HIV-1 by secretory IgA induced by oral immunization with a new macromolecular multicomponent peptide vaccine candidate. Nat. Med. 1:681–685.
Gorse, G. J., Rogers, J. H., Perry, J. E., Newman, F. K., Frey, S. E., Patel, G. B., Belshe, R. B., Schwartz, D. H., Clements, M. L., Keefer, M., Dolin, R., McElrath, J., Corey, L., Graham, B. S., Wright, P. F., Stablein, D. M., Matthews, T. J., Bolognesi, D., Mestecky, J., Walker, M. C., and Fast, P. E. 1995. HIV-1 recombinant gp!60 vaccine-induced antibodies in serum and saliva. Vaccine 13:209–214.
Lin, L., and Putnam, F. W. 1996. Primary structure of the Fc region of human immunoglobulin D: Implications of evolutionary origin and biologic function. Proc. Natl. Acad. Sci. USA 78:504–511.
Melcher, U., Vitetta, E. S., McWilliams, M., Lamm, M. E., Philips-Quagliata, J. M., and Uhr, J. W. 1974. Cell surface immunoglobulin X. Identification of an IgD-like molecule on the surface of murine splenocytes. J. Exp. Med. 140:1427–1435.
Forster, I., Vieira, P., and Rajewsky, K. 1989. Flow cytometric analysis of cell proliferation dynamics in the B cell compartment of the mouse. Int. Immunol. 1:321–331.
Abney, E., and Parkhouse, R. M. 1974. Candidate for immunoglobulin D present on murine B lymphocytes. Nature 253:600–602.
Abney, E., Cooper, M. D., Kearney, J. F., Lawton, A., and Parkhouse, R. M. 1978. Sequential expression of immunoglobulin on developing mouse B lymphocytes. J. Immunol. 120:2041–2050.
Layton, J. E., Johnson, G. R., Scott, D. W., and Nossal, G. J. V., 1978. The ami delta suppressed mouse. Eur. J. Immunol. 8:325–332.
Morris, S. C., Lees, A., and Finkelman, F. D. 1994. In vivo activation of naive T cells by antigen-presenting B cells. J. Immunol. 152:3777–3785.
MacLennan, I. C., Gray, D., Kumararatne, D. S., and Bazin, H. 1982. The lymphocytes of silenic marginal zones: A distinct B-cell lineage. Immunol. Today 3:305–307.
Black, S. J., Van der Loo, W., Loken, M. R., and Herzenberg, L. A. 1978. Expression of IgD by murine lymphocytes: Loss of surface IgD indicates maturation of memory B cells. J. Exp. Med. 147:984–986.
Havran, W. L., DiGiusto, D., and Cambier, J. C. 1984. mIgM:mlgD ratios on B cells: Mean mlgD expression exceeds mIgM by 10-fold on most splenic B cells. J. Immunol. 132:1712–1721.
Brink, R., Goodnow, C.C., and Basten, A. 1995. IgD expression on B cells is more efficient than IgM but both receptors are functionally equivalent in up-regulation CD80/CD86 co-stimulatory molecules. Eur. J. Immunol. 25:1980–1984.
Venkitaraman, A. R., Williams, G. T., Dariavach, P., and Neuberger, M. S. 1991. The B-cell antigen receptor of the five immunoglobulin classes. Nature 352:777–781.
Cooke, M. P., Heath, A. W., Shokat, K. M., Zeng, Y., Finkelman, F. D., Linsley, P. S., Howard, M., and Goodnow, C. C. 1994. Immunoglobulin signal transduction guides the specificity of B cell-T cell interactions and is blocked in tolerant self-reactive B cells. J. Exp. Med. 179:425–438.
Cambier, J. C., and Ransom, J. T. 1987. Molecular mechanisms of transmembrane signaling in B lymphocytes. Annu. Rev. Immunol. 5:175–199.
Brink, R., Goodnow, C. C., Crosbie, J., Adams, E., Eris, J., Mason, D. Y., Hartley, S. B., and Basten, A. 1992. Immunoglobulin M and D antigen receptors are both capable of mediating B lymphocyte activation, deletion, or anergy after interaction with specific antigen. J. Exp. Med. 176:991–1005.
Goodnow, C. C., Crosbie, J., Adelstein, S., Lavoie, T. B., Smith-Gill, S. J., Brink, R. A., Pritchard-Briscoe, H., Wotherspoon, J. S., Loblay, R. H., and Raphael, K. 1988. Altered immunoglobulin expression and functional silencing of self-reactive B lymphocytes in transgenic mice. Nature 334:676–682.
Mason, D. Y., Jones, M., and Goodnow, C. C. 1992. Development and follicular localization of tolerant B lymphocytes in lysozyme/anti-lysozyme IgM/IgD transgenic mice. Int. Immunol. 4:163–175.
Hathcock, K. S., Laszlo, G., Pucillo, C., Linsley, P., and Hodes, R. J. 1994. Comparative analysis of B7-1 and B7-2 costimulatory ligands: Expression and function. J. Exp. Med. 180:631–640.
Kim, K. M., and Reth, M. 1995. The B-cell antigen receptor of class IgD induces a stronger and more prolonged protein-tyrosine phosphorylation than that of class IgM. J. Exp. Med. 181:1005–1014.
Monroe, J. G., Havran, W. L., and Cambier, J. C. 1983. B lymphocyte activation: Entry into cell cycle is accompanied by decreased expression of IgD but not IgM. Eur. J. Immunol. 13:208–213.
Black, S. J., Tokuhisa, T., and Herzenberg, L. A. 1980. Memory B cells at successive stages of differentiation: Expression of surface IgD and capacity for self renewal. Eur. J. Immunol. 10:846–852.
Bhan, A. K., Nadler, L. M., Stashenko, P., McGluskey, R. T., and Schlossman, S. F. 1996. Stages of B cell differentiation in human lymphoid tissue. J. Exp. Med. 154:737–745.
Liu, Y. J., Oldfield, S., and MacLennan, J. C. 1988. Memory B cells in T cell-dependent antibody responses colonize the splenic marginal zones. Eur. J. Immunol. 18:355–362.
McHeyzer Williams, M. G., Nossal, G. J., and Lalor, P. A. 1991. Molecular characterization of single memory B cells. Nature 350:502–505.
Klein, U., Kuppers, R., and Rajewsky, K. 1993. Human IgM+IgD+ B cells, the major B cell subset in the peripheral blood, express V kappa genes with no or little somatic mutation throughout life. Eur. J. Immunol. 23:3272–3277.
Gray, D. 1993. Immunological memory. Annu. Rev. Immunol. 11:49–77.
Gu, H., Tarlinton, D., Muller, W., Rajewsky, K., and Forster, I. 1991. Most peripheral B cells in mice are ligand selected. J. Exp. Med. 173:1357–1371.
Nicholson, I. C., Brisco, M. J., and Zola, H. 1995. Memory B-lymphocytes in human tonsil do not express surface IgD. J. Immunol. 154:1105–1110.
Liu, Y. J., de Bouteiller, O., Arpin, C., Briere, F., Galibert, L., Ho, S., Martinez Valdez, H., Banchereau, J., and Lebecque, S. 1996. Normal human IgD+IgM-germinal center B cells can express up to 80 mutations in the variable region of their IgD transcripts. Immunity 4:603–613.
Zilron, I. M., Mosier, D. E., and Paul, W. E. 1977. The role of surface IgD in the response to thymicindependent antigens. J. Exp. Med. 146:1707–1718.
Cambier, J. C., Ligler, F. S., Uhr, J. W., Kettman, J., and Vietta, E. S. 1978. Blocking of primary in vitro antibody responses to thymus-independent and thymus-dcpcndent antigens with antiserum specific for IgM and IgD. Proc. Natl. Acad. Sci. USA 75:432–439.
Rocs, J., and Rajewsky, K. 1993. Immunoglobulin D (IgD)-deficient mice reveal an auxiliary receptor function for IgD in antigen-mediated recruitment of B cells. J. Exp. Med. 177:45–55.
Nitschke, L., Kosco, M. H., Kohler, G., and Lamers, M. C. 1993. Immunoglobulin D-deficient mice can mount normal immune responses to thymus-independent and-dependent antigens. Proc. Natl. Acad. Sci. USA 90:1887–1891.
Roes, J., and Rajewsky, K. 1991. Cell autonomous expression of IgD is not essential for the maturation of conventional B cells. Int. Immunol. 3:1367–1371.
Netzlin, R. 1990. Internal movements in immunoglobulin molecules. Adv. Immunol. 48:1.
Swenson, C. D., Van Vollenhoven, R. F., Xue, B., Siskind, G. W., Thorbecke, G. J., and Coico, R. F. 1988. Physiology of IgD. IX. Effect of IgD on immunoglobulin production in young and old mice. Eur. J. Immunol. 18:13–20.
Finkelman, F. D., Snapper, C. M., Mountz, J. D., and Katona, I. M. 1987. Polyclonal activation of the murine immune system by a goat antibody to mouse IgD. IX. Induction of a polyclonal IgE response. J. Immunol. 138:2826–2830.
Kricek, F., Ruf, C., Zunic, M., De Jong, G., Dukor, P., and Bahr, G. M. 1995. Induction in mice of serum IgE levels after treatment with anti-mouse IgD antibodies is preceded by differential modulation of tissue cytokine gene transcription. Eur. J. Immunol. 25:936–941.
Matsuzaki, G., Song, F., and Nomoto, K. 1996. Suppression of T-helper type-1 immune response against Listeria-monocytogenes by treatment of mice with goat antibodies to mouse IgD. Immunology 87:15–20.
Dieter, M. P., French, J. E., Boorman, G. A., and Luster, M. I. 1987. Metabolic characterization of mouse bone marrow cells responsive to estrogenic inhibition: Hexose monophosphate shunt enzyme activity in enriched populations of mature cells and progenitor cells. J. Leukoc. Biol. 41:212–219.
Peng, Z., Fisher, R., and Adkinson, N. F., Jr. 1991. Total serum IgD is increased in atopic subjects. Allergy 46:436–444.
Zhang, M, Nichus, J., Brunnee, T., Kleinetebbe, J., O’Connor, A., and Kunkel, G. 1994. Measurement of allergen-specific IgD and correlation with allergen-specific IgE. Scand. J. Immunol. 40:502–508.
Allen, J. E., and Maizels, R. M. 1996. Immunology of human helminth infection. Int. Arch. Allergy Immunol. 109:3–10.
Gouinni, A. S., Lamkhioued, B., Ochiai, K., Tanaka, Y., Delaporte, E., Capron, A., Kinet, J. P., and Capron, M. 1994. High-affinity IgE receptor on eosinophils is involved in defence against parasites. Nature 367:183–186.
Barnes, P. J. 1991. Biochemistry of asthma. Trends Biochem. Sci. 16:365–369.
Mudde, G. C., Bheekha, R., and Bruijnzeelkoomen, C. A. F. M. 1995. IgE-mediated antigen presentation. Allergy 50:193–199.
Robbins, J. B., Schneerson, R., and Szu, S. C. 1995. Perspective:hypothesis:serum IgG antibody is sufficient to confer protection against infectious diseases by inactivating the inoculum. J. Infect. Din. 171:1387–1398.
Papadea, C., and Check, I. J. 1989. Human immunoglobulin G and immunoglobulin G subclasses: Biochemical, genetic, and clinical aspects. Crit. Rev. Clin. Lab. Sci. 27:27–58.
Sun, L., Luce, M. J., Ren, K., Ha, H., and Burrows, P. D. 1995. Identification of polymorphisms in the constant region of IgG3: The missing mouse allotype. Int. Immunol. 7:337–341.
Steinberg, A. G., Morell, A., Skvaril, F., and Van Loghem, E. 1973. The effect of Gm(23) on the concentration of IgG2 and IgG4 in normal human serum. J. Immunol. 110:1642–1651.
Yount, W. J., Kunkel, H. G., and Litwin, S. 1967. Studies of the VI (gamma-2C) subgroup of gamma globulin. A relationship between concentration and genetic type among normal individuals. J. Exp. Med. 125:177–188.
Brekke, O. H., Michaelsen, T. E., and Sandlie, I. 1995. The structural requirements for complement activation by IgG: Does it hinge on the hinge? Immunol. Today 16:85–90.
Dangl, J. L., Wensel, T. G., Morrison, S. L., Stryer, L., Herzenberg, L. A., and Oi, V. T. 1988. Segmental flexibility and complement fixation of genetically engineered chimeric human, rabbit and mouse antibodies. EMBO J. 7:1989–1994.
Winkelhake, J. L. 1978. Immunoglobulin structure and effector function. Immunochemistry 15:695–714.
Tao, M. H., and Morrison, S. L. 1989. Studies of aglycosylated chimeric mouse-human IgG. Role of carbohydrate in the structure and effector functions mediated by the human IgG constant region. J. Immunol. 143:2595–2601.
Huck, S., Fort, P., Crawford, D. H., LeFranc, M. P., and Lefranc, G. 1986. Sequence of a human immunoglobulin gamma 3 heavy chain constant region gene: Comparison with the other human C gamma genes. Nucleic Acids Res. 14:1779–1789.
Brekke, O. H., Michaelsen, T. E., Sandin, R., and Sandlie, I. 1993. Activation of complement by an IgG molecule without a genetic hinge. Nature 363:628–630.
Tan, L. K., Shopes, R. J., Oi, V. T., and Morrison, S. L. 1990. Influence of the hinge region on complement activation, Clq binding, and segmental flexibility in chimeric human immunoglobulins. Proc. Natl. Acad. Sci. USA 87:162–166.
Norderhaug, L., Brekke, O. H., Bremnes, B,, Sandin, R., Aase, A., Michaelsen, T. E., and Sandlie, I. 1991. Chimeric mouse human IgG3 antibodies with an IgG4-like hinge region induce complement-mediated lysis more efficiently than IgG3 with normal hinge. Eur. J. Immunol. 21:2379–2384.
Clynes, R., and Ravetch, J. V. 1995. Cytotoxic antibodies trigger inflammation through Fc receptors. Immunity 3:21–26.
Ales Martinez., J. E., Cuende, E., Martinez, C., Parkhouse, R. M., Pezzi, L., and Scott, D. W. 1991. Signalling in B cells. Immunol. Today 12:201–205.
Goding, J. M., and Layton, J. E. 1976. Antigen-induced co-capping of IgM and IgD-like receptors on murine B cells. J. Exp. Med. 144:852–857.
Goodnow, C. C., Crosbie, J., Jorgensen, H., Brink, R. A., and Basten, A. 1989. Induction of self-tolerance in mature peripheral B lymphocytes. Nature 342:385–391.
Monteiro, R. C., Hostoffer, R. W., Cooper, M. D., Bonner, J. R., Gartland, G. L., and Kubagawa, H. 1993. Definition of immunoglobulin A receptors on eosinophils and their enhanced expression in allergic individuals. J. Clin. Invest. 92:1681–1685.
Monteiro, R. C., Kubagawa, H., and Cooper, M. D. 1990. Cellular distribution, regulation, and biochemical nature of an Fc alpha receptor in humans. J. Exp. Med. 171:597–613.
Patry, C, Sibille, Y., Lehuen, A., and Monteiro, R. C. 1996. Identification of Fc-alpha receptor (CD89) isoforms generated by alternative splicing that are differentially expressed between blood monocytes and alveolar macrophages. J. Immunol. 156:4442–4448.
Sibille, Y., Chatelain, B., Staquet, P., Merrill, W. W., Delacroix, D. L., and Vaerman, J. P. 1989. Surface IgA and Fc-alpha receptors on human alveolar macrophages from normal subjects and from patients with sarcoidosis. Am. Rev. Respir. Dis. 139:740–747.
Albrechtsen, M., Yeaman, G. R., and Kerr, M. A. 1988. Characterization of the IgA receptor from human polymorphonuclear leucocytes. Immunology 64:201–205.
Pfefferkorn, L. C., and Yeaman, G. R. 1994. Association of IgA-Fc receptors (Fc alpha R) with Fc epsilon RI gamma 2 subunits in U937 cells. Aggregation induces the tyrosine phosphorylation of gamma 2. J. Immunol. 153:3228–3236.
Patry, C., Herbelin, A., Lehuen, A., Bach, J. F., and Monteiro, R. C. 1995. Fc alpha receptors mediate release of tumour necrosis factor-alpha and interleukin-6 by human monocytes following receptor aggregation. Immunology 86:1–5.
Shen, L. 1992. Receptors for IgA on phagocytic cells. Immunol. Res. 11:273–282.
Hostoffer, R. W., Krukovets, I., and Berger, M. 1994. Enhancement of tumor necrosis factor-alpha of Fc alpha receptor expression and IgA-mediated superoxide generation and killing of Pseudomonas aeruginosa by polymorphonuclear leukocytes. J Infect. Dis. 170:82–87.
Reterink, T. J., Levarht, E. W., Klar Mohamad, N., van Es, L. A., and Daha, M. R. 1996. Transforming growth factor-beta 1 (TGF-beta 1) down-regulates IgA Fc-receptor (CD89) expression on human monocytes. Clin. Exp. Immunol. 103:161–166.
Grossetete, B., Viard, J. P., Lehuen, A., Bach, J. F., and Monteiro, R. C. 1995. Impaired Fc alpha receptor expression is linked to increased immunoglobin A levels and disease progression in HIV-1-infected patients. AIDS 9:229–234.
Carayannopoulos, L., Hexham, J. M., and Capra, J. D. 1996. Localization of the binding site for the monocyte immunoglobulin (Ig) A-Fc receptor (CD89) to the domain boundary between Calpha2 and Calpha3 in human IgA1. J. Exp. Med. 183:1579–1586.
Vandijk, T. B., Bracke, M., Caldenhoven, E., Raaijmakers, J. A. M., and Lammers, J. W. J. 1996. Cloning and characterization of FcalphaRb, a novel Fc-alpha receptor (CD89) isoform expressed in eosinophils and neutrophils. Blood 88:4229–4238.
Marshall, J. S., and Bienenstock, J. 1994. The role of mast cells in inflammatory reactions of the airways, skin and intestine. Curr. Opin. Immunol. 6:853–859.
Daeeron, M., Malbec, O., Latour, S., Arock, M., and Fridman, W. H. 1995. Regulation of high-affinity IgE receptor-mediated mast cell activation by murine low-affinity IgG receptors. J. Clin. Invest. 95:577–585.
Weber, S., Krueger Krasagakes, S., Grabbe, J., Zuberbier, T., and Czarnetzki, B. M. 1995. Mast cells. Int. J. Dermatol. 34:1–10.
Wang, B., Rieger, A., Kilgus, O., Ochiai, K., Maurer, D., Foedinger, D., Kinet, J. P., and Stingl, G. 1992. Epidermal Langerhans cells from normal human skin bind monomeric IgE via Fc epsilon RI. J. Exp. Med. 175:1353–1365.
Bieber, T., de la Salle, H., Wollenberg, A., Hakimi, J., Chizzonite, R., Ring, J., Hanau, D., and de la Salle, C. 1992. Human epidermal Langerhans cells express the high affinity receptor for immunoglobulin E (Fc epsilon RI). J. Exp. Med. 175:1285–1290.
Bieber, T. 1994. Fc epsilon RI on human Langerhans cells: A receptor in search of new functions. Immunol. Today 15:52–53.
Maurer, D., and Stingl, G. 1995. Immunoglobulin E-binding structures on antigen-presenting cells present in skin and blood. J. Invest. Dermatol. 104:707–710.
Knol, E. F., Verhoeven, A. J., and Roos, D. 1993. Stimulus secretion coupling in human basophilic granulocytes. Clin. Exp. Allergy 23:471–480.
Schroeder, J. T., Kagey Sobotka, A., and Lichtenstein, L. M. 1995. The role of the basophil in allergic inflammation. Allergy 50:463–472.
Capron, M., Soussi Gounni, A., Morita, M., Truong, M. J., Prin, L., Kinet, J. P., and Capron, A. 1995. Eosinophils: From low-to high-affinity immunoglobulin E receptors. Allergy 50:20–23.
Gounni, A. S., Lamkhioued, B., Delaporte, E., Dubost, A., Kinet, J. P., Capron, A., and Capron, M. 1994. The high-affinity IgE receptor on eosinophils: From allergy to parasites or from parasites to allergy? J. Allergy Clin. Immunol. 94:1214–1216.
Hashimoto, S., Koh, K., Tomita, Y., Amemiya, E., Sawada, S., Yodoi, J., and Horie, T. 1995. TNF-alpha regulates IL-4-induced Fc epsilon RII/CD23 gene expression and soluble Fc epsilon RII release by human monocytes. Int. Immunol. 7:705–713.
Edberg, J. C., Lin, C. T., Lau, D., Unkeless, J. C., and Kimberly, R. P. 1995. The Ca2+ dependence of human Fc gamma receptor-initiated phagocytosis. J. Biol. Chem. 270:22301–22307.
Lecoanet Henchoz, S., Gauchat, J. F., Aubry, J. P., Graber, P., Life, P., Paul Eugene, N., Ferrua, B., Corbi, A. L., Dugas, B., Plater Zyberk, C., and Bonnefoy, J. Y. 1995. CD23 regulates monocyte activation through a novel interaction with the adhesion molecules CD11b-CD18 and CD11c-CD18. Immunity 3:119–125.
Maurer, D., Ebner, C., Reininger, B., Fiebiger, E., Kraft, D., Kinet, J. P., and Stingl, G. 1995. The high affinity IgE receptor (Fc epsilon R1) mediates IgE-dependent allergen presentation. J. Immunol. 154:6285–6290.
Ra, C., Jouvin, M. H., Blank, U., and Kinet, J. P. 1989. A macrophage Fc gamma receptor and the mast cell receptor for IgE share an identical subunit. Nature 341:752–754.
Beaven, M. A., and Metzger, H. 1993. Signal transduction by Fc receptors: The Fc epsilon RI case. Immunol. Today 14:222–226.
Blank, U., Ra, C., Miller, L., White, K., Metzger, H., and Kinet, J. P. 1989. Complete structure and expression in transfected cells of high affinity IgE receptor. Nature 337:187–189.
Dombrowicz, D., Flamand, V., Brigman, K. K., Roller, B. H., and Kinet, J. P. 1993. Abolition of anaphylaxis by targeted disruption of the high affinity immunoglobulin E receptor alpha chain gene. Cell 75:969–976.
Takai, T., Li, M., Sylvestre, D., Clynes, R., and Ravetch, J. V. 1994. FcR gamma chain deletion results in pleiotrophic effector cell defects. Cell 76:519–529.
Hagen, M., Sacco, R. E., Sandor, M., Best, C., Nambu, M., and Lynch, R. G. 1995. The Fc epsilon RII/CD23 gene is actively transcribed during all stages of murine B-lymphocyte development. Mol. Immunol. 32:1245–1257.
Zhang, H. M., Tanaka, Y., Maeda, K., Anan, S., and Yoshida, H. 1996. Affinity-purified Dermatophagoides farinae antigen induces CD23 on T and B lymphocytes and monocytes specifically in patients with atopic dermatitis. J. Dermatol. Sci. 11:202–208.
Carini, C., and Fratazzi, C. 1996. CD23 expression in activated human T cells is enhanced by interleukin-7. Int. Arch. Allergy Immunol. 110:23–30.
Yokota, A., Yukawa, K., Yamamoto, A., Sugiyama, K., Suemura, M., Tashiro, Y., Kishimoto, T., and Kikutani, H. 1992. Two forms of the low-affinity Fc receptor for IgE differentially mediate endocytosis and phagocytosis: Identification of the critical cytoplasmic domains. Proc. Natl. Acad. Sci. USA 89:5030–5034.
Sarfati, M., Fournier, S., Wu, C. Y., and Delespesse, G. 1992. Expression, regulation and function of human Fc epsilon RII (CD23) antigen. Immunol. Res. 11:260–272.
Yu, P., Kosco Vilbois, M., Richards, M., Kohler, G., and Lamers, M. C. 1994. Negative feedback regulation of IgE synthesis by murine CD23. Nature 369:753–756.
Bonnefoy, J. Y., Gauchat, J. F., Life, P., Graber, P., Aubry, J. P., and Lecoanet Henchoz, S. 1995. Regulation of IgE synthesis by CD23/CD21 interaction. Int. Arch. Allergy Immunol. 107:40–42.
Fujiwara, H., Kikutani, H., Suematsu, S., Naka, T., Yoshida, K., Tanaka, T., Suemura, M., Matsumoto, N., Kojima, S., et al. 1994. The absence of IgE antibody-mediated augmentation of immune responses in CD23-deficient mice. Proc. Natl. Acad. Sci. USA 91:6835–6839.
Fremeaux Bacchi, V., Bernard, I., Maillet, F., Mani, J. C., Fontaine, M., Bonnefoy, J. Y., Kazatchkine, M. D., and Fischer, E. 1996. Human lymphocytes shed a soluble form of CD21 (the C3dg/Epstein-Barr virus receptor, CR2) that binds iC3b and CD23. Eur. J. Immunol. 26:1497–1503.
Henchoz Lecoanet, S., Jeannin, P., Aubry, J. P., Graber, P., Bradshaw, C. G., Pochon, S., and Bonnefoy, J. Y. 1996. The Epstein-Barr virus-binding site on CD21 is involved in CD23 binding and interleukin-4-induced IgE and IgG4 production by human B cells. Immunology 88:35–39.
Dugas, N., Vouldoukis, I., Becherel, P., Arock, M., Debre, P., Tardieu, M., Mossalayi, D. M., Delfraissy, J. F., Kolb, J. P., and Dugas, B. 1996. Triggering of CD23b antigen by anti-CD23 monoclonal antibodies induces interleukin-10 production by human macrophages. Eur. J. Immunol. 26:1394–1398.
Dugas, B., Mossalayi, M. D., Damais, C., and Kolb, J. P. 1995. Nitric oxide production by human monocytes: Evidence for a role of CD23. Immunol. Today 16:574–580.
Yamaoka, K. A., Arock, M., Issaly, F., Dugas, N., Le Goff, L., and Kolb, J. P. 1996. Granulocyte macrophage colony stimulating factor induces Fc epsilon RII/CD23 expression on normal human polymorphonuclear neutrophils. Int. Immunol. 8:479–490.
Paterson, R. L., Lack, G., Domenico, J. M., Delespesse, G., Leung, D. Y., Finkel, T. H., and Gelfand, E. W. 1996. Triggering through CD40 promotes interleukin-4-induced CD23 production and enhanced soluble CD23 release in atopic disease. Eur. J. Immunol. 26:1979–1984.
Kaufmann, Y., Golstein, P., Pierres, M., Springer, T. A., and Eshhar, Z. 1982. LFA-I but not Lyt-2 is associated with killing activity of cytotoxic T lymphocyte hybridomas. Nature 300:357–360.
Burlinson, E. L., Graber, P., Bonnefoy, J. Y., Ozanne, B. W., and Cushley, W. 1996. Soluble CD40 ligand induces expression of CD25 and CD23 in resting human tonsillar B lymphocytes. Eur. J. Immunol. 26:1069–1073.
Ruzek, M. C., Billadeau, D., and Mathur, A. 1996. A combination of IL-10 and direct contact with plasma cell tumors decreases CD23 expression on splenic B cells. J. Immunol. 156:2124–2132.
Kimberly, R. P., Salmon, J. E., and Edberg, J. C. 1995. Receptors for immunoglobulin G. Molecular diversity and implications for disease. Arthritis Rheum. 38:306–314.
Unkeless, J. C., Shen, Z., Lin, C. W., and DeBeus, E. 1995. Function of human Fc gamma RIIA and Fc gamma RI1IB. Semin. Immunol. 7:37–44.
Indik, Z. K., Park, J. G., Hunter, S., and Schreiber, A. D. 1995. Structure/function relationships of Fc gamma receptors in phagocytosis. Semin. Immunol. 7:45–54.
Fanger, M. W., and Erbe, D. V. 1992. Fc gamma receptors in cancer and infectious disease. Immunol. Res. 11:203–216.
Unkeless, J. C. 1989. Function and heterogeneity of human Fc receptors for immunoglobulin G. J. Clin. Invest. 83:355–361.
Landor, M. 1995. Maternal-fetal transfer of immunoglobulins. Ann. Allergy Asthma Immunol. 74:279–283.
Saji, F., Koyama, M., and Matsuzaki, N. 1994. Current topic: Human placenta) Fc receptors. Placenta 15:453–466.
Galon, J., Bouchard, C., Fridman, W. H., and Sautes, C. 1995. Ligands and biological activities of soluble Fc gamma receptors. Immunol. Lett. 44:175–181.
Hartnell, A., Kay, A. B., and Wardlaw, A. J. 1992. IFN-gamma induces expression of Fc gamma RIII (CD16) on human eosinophils. J. Immunol. 148:1471–1478.
Pan, L. Y., Mendel, D. B., Zurlo, J., and Guyre, P. M. 1990. Regulation of the steady state level of Fc gamma RI mRNA by IFN-gamma and dexamethasone in human monocytes, neutrophils, and U-937 cells. J. Immunol. 145:267–275.
Olweus, J., Lund Johansen, F., and Terstappen, L. W. 1995. CD64/Fc gamma RI is a granulo-monocytic lineage marker on CD34+ hematopoietic progenitor cells. Blood 85:2402–2413.
Unkeless, J. C., Scigliano, E., and Freedman, V. H. 1988. Structure and function of human and murine receptors for IgG. Annu. Rev. Immunol. 6:251–281.
Sivo, J., Politis, A. D., and Vogel, S. N. 1993. Differential effects of interferon-gamma and glucocorticoids on Fc gamma R gene expression in murine macrophages. J. Leukoc. Biol. 54:451–457.
Prins, J. B., Todd, J. A., Rodrigues, N. R., Ghosh, S., Hogarth, P. M., Wicker, L. S., Gaffney, E., Podolin, P. L., Fischer, P. A., Sirotina, A., et al. 1993. Linkage on chromosome 3 of autoimmune diabetes and defective Fc receptor for IgG in NOD mice. Science 260:695–698.
Teillaud, J. L., Bouchard, C., Astier, A., Teillaud, C., Tartour, E., Michon, J., Galinha, A., Moncuit, J., Mazieres, N., and Spagnoli, R. 1994. Natural and recombinant soluble low-affinity Fc gamma R: Detection, purification, and functional activities. Immunomelhods 4:48–64.
Takizawa, F., Adamczewski, M., and Kinet, J. P. 1992. Identification of the low affinity receptor for immunoglobulin E on mouse mast cells and macrophages as Fc gamma RII and Fc gamma RIII. J. Exp. Med. 176:469–475.
Hulett, M. D., and Hogarth, P. M. 1994. Molecular basis of Fc receptor function. Adv. Immunol. 57:1–127.
Mantzioris, B. X., Berger, M. F., Sewell, W., and Zola, H. 1993. Expression of the Fc receptor for IgG (Fc gamma RII/CDw32) by human circulating T and B lymphocytes. J. Immunol. 150:5175–5184.
Schmitt, D. A., Hanau, D., Bieber, T., Dezutter Dambuyant, C., Schmitt, D., Fabre, M., Pauly, G., and Cazenave, J. P. 1990. Human epidermal Langerhans cells express only the 40-kilodalton Fc gamma receptor (FcRII). J. Immunol. 144:4284–4290.
Vaughn, M., Taylor, M., and Mohanakumar, T. 1985. Characterization of human IgG Fc receptors. J. Immunol. 135:4059–4065.
Katz, H. R., Arm, J. P., Benson, A. C., and Austen, K. F. 1990. Maturation-related changes in the expression of Fc gamma RIII and Fc gamma RII on mouse mast cells derived in vitro and in vivo. J. Immunol. 145:3412–3417.
Edberg, J. C., Redecha, P. B., Salmon, J. E., and Kimberly, R. P. 1989. Human Fc gamma RIII (CD16). Isoforms with distinct allelic expression, extracellular domains, and membrane linkages on polymorphonuclear and natural killer cells. J. Immunol. 143:1642–1649.
Weinshank, R. L., Luster, A. D., and Ravetch, J. V. 1988. Function and regulation of a murine macrophage-specific IgG Fc receptor, Fc gamma R-alpha. J. Exp. Med. 167:1909–1925.
Clarkson, S. B., Kimberly, R. P., Valinsky, J. E., Witmer, M. D., Bussel, J. B., Nachman, R. L., and Unkeless, J. C. 1986. Blockade of clearance of immune complexes by an anti-Fc gamma receptor monoclonal antibody. J. Exp. Med. 164:474–489.
Buckle, A. M., and Hogg, N. 1989. The effect of IFN-gamma and colony-stimulating factors on the expression of neutrophil cell membrane receptors. J. Immunol. 143:2295–2301.
Solvason, N., and Kearney, J. F. 1992. The human fetal omentum: A site of B cell generation. J. Exp. Med. 175:397–404.
Rolink, A., Haasner, D., Nishikawa, S., and Melchers, F. 1993. Changes in frequencies of clonable pre B cells during life in different lymphoid organs of mice. Blood 81:2290–2300.
Rajewsky, K. 1992. Early and late B-cell development in the mouse. Curr. Opin. Immunol. 4:171–176.
Tsubata, T., and Nishikawa, S. 1991. Molecular and cellular aspects of early B-cell development. Curr. Opin. Immunol. 3:186–192.
Rolink, A., and Melchers, F. 1993. Generation and regeneration of cells of the B-lymphocyte lineage. Curr. Opin. Immunol. 5:207–217.
Osmond, D. G. 1991. Proliferation kinetics and the lifespan of B cells in central and peripheral lymphoid organs. Curr. Opin. Immunol. 3:179–185.
Davis, S. J., Davies, E. A., Barclay, A. N., Daenke, S., Bodine, D., Jones, E. Y., Stuart, D. I., Butters, T. D., Dwek, R. A., and Van-der-Merwe, P. A. 1995. Ligand binding by the immunoglobulin superfamily recognition molecule CD2 is glycosylation-independent. J. Biol. Chem. 270:369–375.
Wright, A., Tao, M. H., Kabat, E. A., and Morrison, S. L. 1991. Antibody variable region glycosylation: Position effects on antigen binding and carbohydrate structure. EMBO J. 10:2717–2723.
Middaugh, C. R., and Litman, G. W. 1987. Atypical glycosylation of an IgG monoclonal cryoimmunoglobulin. J. Biol. Chem. 262:3671–3673.
Co, M. S., Scheinberg, D. A., Avdalovic, N. M., McGraw, K., Vasquez, M., Caron, P. C., and Queen, C. 1993. Genetically engineered deglycosylation of the variable domain increases the affinity of an anti-CD33 monoclonal antibody. Mol. Immunol. 30:1361–1367.
Miletic, V. D., and Frank, M. M. 1995. Complement immunoglobulin interactions. Curr. Opin. Immunol. 7:41–47.
Wright, A., and Morrison, S. L. 1994. Effect of altered CH2-associated carbohydrate structure on the functional properties and in vivo fate of chimeric mouse-human immunoglobulin GI. J. Exp. Med. 180:1087–1096.
Tao, M. H., and Morrison, S. L. 1989. Studies of aglycosylated chimeric mouse-human IgG. Role of carbohydrate in the structure and effector functions mediated by the human IgG constant region. J. Immunol. 143:2595–2601.
Axford, J. S., Sumar, N., Alavi, A., Isenberg, D. A., Young, A., Bodman, K. B., and Roitt, I. M. 1992. Changes in normal glycosylation mechanisms in autoimmune rheumatic disease. J. Clin. Invest. 89:1021–1031.
Roccatello, D., Picciotto, G., Torchio, M., Ropolo, R., Ferro, M., Franceschini, R., Quattrocchio, G., Cacace, G., and Coppo, R. 1993. Removal systems of immunoglobulin A and immunoglobulin A containing complexes in IgA nephropathy and cirrhosis patients. The role of asialoglycoprotein receptors, Lab. Invest. 69:714–723.
Andre, P. M., Le Pogamp, P., and Chevet, D. 1990. Impairment of jacalin binding to serum IgA in IgA nephropathy. J. Clin. Lab. Anal. 4:115–119.
Tomlinson, I. M., Walter, G., Jones, P. T., Dear, P. H., Sonnhammer, E. L. L., and Winter, G. 1996. The imprint of somatic hypermutation on the repertoire of human germline-v genes. J. Mot. Biol. 256:813–817.
Hashimoto, S., Gregersen, P. K., and Chiorazzi, N. 1993. The human Ig-beta cDNA sequence, a homologue of murine B29, is identical in B cell and plasma cell lines producing all the human Ig isotypes. J. Immunol. 150:491–498.
Mestecky, J. 1988. Immunobiology of IgA. Am. J. Kidney Dis. 12:378–383.
Papadea, C., and Check, I. J. 1989. Human immunoglobulin G and immunoglobulin G subclasses: Biochemical, genetic, and clinical aspects. Crit. Rev. Clin. Lab. Sci. 27:27–58.
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(1998). B-Lymphocyte Genes. In: Handbook of Imune Response Genes. Springer, Boston, MA. https://doi.org/10.1007/978-0-585-31180-7_4
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